CG010 Proteomics
Faculty of ScienceAutumn 2024
- Extent and Intensity
- 2/0/0. 2 credit(s) (plus 2 credits for an exam). Type of Completion: zk (examination).
In-person direct teaching - Teacher(s)
- doc. Mgr. Jan Havliš, Dr. (lecturer)
prof. RNDr. Zbyněk Zdráhal, Dr. (lecturer)
Mgr. David Potěšil, Ph.D. (lecturer)
Mgr. Tomáš Klumpler, Ph.D. (lecturer)
doc. Mgr. Jan Paleček, Dr. rer. nat. (lecturer) - Guaranteed by
- doc. Mgr. Jan Havliš, Dr.
National Centre for Biomolecular Research – Faculty of Science
Supplier department: National Centre for Biomolecular Research – Faculty of Science - Timetable
- Tue 9:00–10:50 C02/211
- Prerequisites
- basics in biochemistry, analytical and physical chemistry
- Course Enrolment Limitations
- The course is also offered to the students of the fields other than those the course is directly associated with.
- fields of study / plans the course is directly associated with
- Genomics and Proteomics (programme PřF, N-BCH)
- Course objectives
- major goal of this subject is to acquaint students overall and generally with proteomics as a field, with its content and main aspects.
- Learning outcomes
- at the end of the course students should be able:
to understand and to explain terms related to proteomics (protein biosynthesis, sequence, structure, and interactions);
to know relations between protein properties and methods of their study
to use this knowledge on proteins and their complexes to follow their role in organisms. - Syllabus
- Jan Havliš
- Introduction into proteomics – definition of proteome and proteomics. Why it is so important to study proteome and its changes: postgenomic era and what to do with information, which we cannot read, genotype vs. phenotype, what does happen during expression, from gene to protein and back. Approaches of contemporary proteomics: Expression, purification and analysis of recombinant proteins, analysis of relations between structure and function, differential proteomics, analysis of post-translational modifications
- Proteins - biosynthesis of proteins, basic structure hierarchy, basic protein properties (size and shape, polarity, charge, reactivity). Expression proteomics - the conditions and regulation of gene products expression (under different conditions, also ontogenically), protein identity: protoprotein, protein splicing (intein, extein), post-translational modifications, transport, localisation of proteins (eg. cell membrane proteins, secretome), degradation, relations between genotype and phenotype.
- Tomáš Klumpler
- structural proteomics - domains, tertiary structure, protein folding, structure and environment relations, allostery, structure modelling
- Jan Paleček
- Protein interactions - domains, surface - bond types - interactome (maps, evolution) - protein complexes - principles of assembly, modules - molecular machines.
- David Potěšil
- Bioinformatics and proteins - Mw, pI, primary structure, PTMs, domains, tertiary structure, gene ontology (GO), phylogenetic similarity (mutations, proteins from organisms with unsequenced genomes), protein complexes.
- Zbyněk Zdráhal
- Importance and utilisation of proteomics - role of proteomics in basic research, application of proteomics (disease diagnostics, pathogene identification)
- Literature
- Teaching methods
- the lecture is based on ppt presentations and their explication. presentations themselves will be available as study material. it is recommended to attend the lecture, because of the explication, which significantly extends the presentations, and because of the limited availability of textbooks in czech covering certain parts of the subject.
at the beginning of the course, the document containing voluntary running tasks to consolidate the acquired knowledge will be uploaded to the study materials section. - Assessment methods
- the basic written examination takes 90 minutes and consists of a single-choice test with sixty questions, five choices per question. to pass the test, it is necessary to answer correctly at least 60 % of the questions; the test covers the complete content of the course. the examination will conclude with an oral examination consisting of two basic questions.
during the course, students will be given ungraded, voluntary, time-saving tasks to consolidate the acquired knowledge. - Language of instruction
- Czech
- Further Comments
- Study Materials
The course is taught annually. - Listed among pre-requisites of other courses
CG010 Proteomics
Faculty of ScienceAutumn 2023
- Extent and Intensity
- 2/0/0. 2 credit(s) (plus 2 credits for an exam). Type of Completion: zk (examination).
- Teacher(s)
- doc. Mgr. Jan Havliš, Dr. (lecturer)
prof. RNDr. Zbyněk Zdráhal, Dr. (lecturer)
Mgr. David Potěšil, Ph.D. (lecturer)
Mgr. Tomáš Klumpler, Ph.D. (lecturer)
doc. Mgr. Jan Paleček, Dr. rer. nat. (lecturer) - Guaranteed by
- doc. Mgr. Jan Havliš, Dr.
National Centre for Biomolecular Research – Faculty of Science
Supplier department: National Centre for Biomolecular Research – Faculty of Science - Timetable
- Tue 9:00–10:50 C02/211
- Prerequisites
- basics in biochemistry, analytical and physical chemistry
- Course Enrolment Limitations
- The course is also offered to the students of the fields other than those the course is directly associated with.
- fields of study / plans the course is directly associated with
- Genomics and Proteomics (programme PřF, N-BCH)
- Course objectives
- major goal of this subject is to acquaint students overall and generally with proteomics as a field, with its content and main aspects.
- Learning outcomes
- at the end of the course students should be able:
to understand and to explain terms related to proteomics (protein biosynthesis, sequence, structure, and interactions);
to know relations between protein properties and methods of their study
to use this knowledge on proteins and their complexes to follow their role in organisms. - Syllabus
- Jan Havliš
- Introduction into proteomics – definition of proteome and proteomics. Why it is so important to study proteome and its changes: postgenomic era and what to do with information, which we cannot read, genotype vs. phenotype, what does happen during expression, from gene to protein and back. Approaches of contemporary proteomics: Expression, purification and analysis of recombinant proteins, analysis of relations between structure and function, differential proteomics, analysis of post-translational modifications
- Proteins - biosynthesis of proteins, basic structure hierarchy, basic protein properties (size and shape, polarity, charge, reactivity). Expression proteomics - the conditions and regulation of gene products expression (under different conditions, also ontogenically), protein identity: protoprotein, protein splicing (intein, extein), post-translational modifications, transport, localisation of proteins (eg. cell membrane proteins, secretome), degradation, relations between genotype and phenotype.
- Tomáš Klumpler
- structural proteomics - domains, tertiary structure, protein folding, structure and environment relations, allostery, structure modelling
- Jan Paleček
- Protein interactions - domains, surface - bond types - interactome (maps, evolution) - protein complexes - principles of assembly, modules - molecular machines.
- David Potěšil
- Bioinformatics and proteins - Mw, pI, primary structure, PTMs, domains, tertiary structure, gene ontology (GO), phylogenetic similarity (mutations, proteins from organisms with unsequenced genomes), protein complexes.
- Zbyněk Zdráhal
- Importance and utilisation of proteomics - role of proteomics in basic research, application of proteomics (disease diagnostics, pathogene identification)
- Literature
- Teaching methods
- the lecture is based on ppt presentations and their explication. presentations themselves will be available as study material. it is recommended to attend the lecture, because of the explication, which significantly extends the presentations, and because of the limited availability of textbooks in czech covering certain parts of the subject.
at the beginning of the course, the document containing voluntary running tasks to consolidate the acquired knowledge will be uploaded to the study materials section. - Assessment methods
- the basic written examination takes 90 minutes and consists of a single-choice test with sixty questions, five choices per question. to pass the test, it is necessary to answer correctly at least 60 % of the questions; the test covers the complete content of the course. the examination will conclude with an oral examination consisting of two basic questions.
during the course, students will be given ungraded, voluntary, time-saving tasks to consolidate the acquired knowledge. - Language of instruction
- Czech
- Further Comments
- Study Materials
The course is taught annually. - Listed among pre-requisites of other courses
CG010 Proteomics
Faculty of ScienceAutumn 2022
- Extent and Intensity
- 2/0/0. 2 credit(s) (plus 2 credits for an exam). Type of Completion: zk (examination).
- Teacher(s)
- doc. Mgr. Jan Havliš, Dr. (lecturer)
prof. RNDr. Zbyněk Zdráhal, Dr. (lecturer)
Mgr. David Potěšil, Ph.D. (lecturer)
Mgr. Tomáš Klumpler, Ph.D. (lecturer)
doc. Mgr. Jan Paleček, Dr. rer. nat. (lecturer) - Guaranteed by
- doc. Mgr. Jan Havliš, Dr.
National Centre for Biomolecular Research – Faculty of Science
Supplier department: National Centre for Biomolecular Research – Faculty of Science - Timetable
- Tue 9:00–10:50 C02/211
- Prerequisites
- basics in biochemistry, analytical and physical chemistry
- Course Enrolment Limitations
- The course is also offered to the students of the fields other than those the course is directly associated with.
- fields of study / plans the course is directly associated with
- Genomics and Proteomics (programme PřF, N-BCH)
- Course objectives
- major goal of this subject is to acquaint students overall and generally with proteomics as a field, with its content and main aspects.
- Learning outcomes
- at the end of the course students should be able:
to understand and to explain terms related to proteomics (protein biosynthesis, sequence, structure, and interactions);
to know relations between protein properties and methods of their study
to use this knowledge on proteins and their complexes to follow their role in organisms. - Syllabus
- Jan Havliš
- Introduction into proteomics – definition of proteome and proteomics. Why it is so important to study proteome and its changes: postgenomic era and what to do with information, which we cannot read, genotype vs. phenotype, what does happen during expression, from gene to protein and back. Approaches of contemporary proteomics: Expression, purification and analysis of recombinant proteins, analysis of relations between structure and function, differential proteomics, analysis of post-translational modifications
- Proteins - biosynthesis of proteins, basic structure hierarchy, basic protein properties (size and shape, polarity, charge, reactivity). Expression proteomics - the conditions and regulation of gene products expression (under different conditions, also ontogenically), protein identity: protoprotein, protein splicing (intein, extein), post-translational modifications, transport, localisation of proteins (eg. cell membrane proteins, secretome), degradation, relations between genotype and phenotype.
- Tomáš Klumpler
- structural proteomics - domains, tertiary structure, protein folding, structure and environment relations, allostery, structure modelling
- Jan Paleček
- Protein interactions - domains, surface - bond types - interactome (maps, evolution) - protein complexes - principles of assembly, modules - molecular machines.
- David Potěšil
- Bioinformatics and proteins - Mw, pI, primary structure, PTMs, domains, tertiary structure, gene ontology (GO), phylogenetic similarity (mutations, proteins from organisms with unsequenced genomes), protein complexes.
- Zbyněk Zdráhal
- Importance and utilisation of proteomics - role of proteomics in basic research, application of proteomics (disease diagnostics, pathogene identification)
- Literature
- Teaching methods
- the lecture is based on ppt presentations and their explication. presentations themselves will be available as study material. it is recommended to attend the lecture, because of the explication, which significantly extends the presentations, and because of the limited availability of textbooks in english covering certain parts of the subject.
- Assessment methods
- the basic written examination takes 90 minutes and consists of a single-choice test with sixty questions, five choices per question. to pass the test, it is necessary to answer correctly at least 60 % of the questions; the test covers the complete content of the course. the examination will conclude with an oral examination.
during the course, students will be given ungraded, voluntary, time-saving tasks to consolidate the acquired knowledge. - Language of instruction
- Czech
- Further comments (probably available only in Czech)
- Study Materials
The course is taught annually. - Listed among pre-requisites of other courses
- Teacher's information
- 21., 28. 9. a 5. 10. 2020 - jan havliš 12. 10. a 19. 10. 2020 - tomáš klumpler 26. 10. a 2. 11. 2020 - honza paleček 9. 11. a 16. 11. 2020 - david potěšil 23. 11. 2020 - zbyněk dráhal
CG010 Proteomics
Faculty of Scienceautumn 2021
- Extent and Intensity
- 2/0/0. 2 credit(s) (plus 2 credits for an exam). Type of Completion: zk (examination).
- Teacher(s)
- doc. Mgr. Jan Havliš, Dr. (lecturer)
prof. RNDr. Zbyněk Zdráhal, Dr. (lecturer)
Mgr. David Potěšil, Ph.D. (lecturer)
Mgr. Tomáš Klumpler, Ph.D. (lecturer)
doc. Mgr. Jan Paleček, Dr. rer. nat. (lecturer) - Guaranteed by
- doc. Mgr. Jan Havliš, Dr.
National Centre for Biomolecular Research – Faculty of Science
Supplier department: National Centre for Biomolecular Research – Faculty of Science - Timetable
- Tue 9:00–10:50 C02/211
- Prerequisites
- basics in biochemistry, analytical and physical chemistry
- Course Enrolment Limitations
- The course is also offered to the students of the fields other than those the course is directly associated with.
- fields of study / plans the course is directly associated with
- Genomics and Proteomics (programme PřF, N-BCH)
- Course objectives
- major goal of this subject is to acquaint students overall and generally with proteomics as a field, with its content and main aspects.
- Learning outcomes
- at the end of the course students should be able:
to understand and to explain terms related to proteomics (protein biosynthesis, sequence, structure, and interactions);
to know relations between protein properties and methods of their study
to use this knowledge on proteins and their complexes to follow their role in organisms. - Syllabus
- Jan Havliš
- Introduction into proteomics – definition of proteome and proteomics. Why it is so important to study proteome and its changes: postgenomic era and what to do with information, which we cannot read, genotype vs. phenotype, what does happen during expression, from gene to protein and back. Approaches of contemporary proteomics: Expression, purification and analysis of recombinant proteins, analysis of relations between structure and function, differential proteomics, analysis of post-translational modifications
- Proteins - biosynthesis of proteins, basic structure hierarchy, basic protein properties (size and shape, polarity, charge, reactivity). Expression proteomics - the conditions and regulation of gene products expression (under different conditions, also ontogenically), protein identity: protoprotein, protein splicing (intein, extein), post-translational modifications, transport, localisation of proteins (eg. cell membrane proteins, secretome), degradation, relations between genotype and phenotype.
- Tomáš Klumpler
- structural proteomics - domains, tertiary structure, protein folding, structure and environment relations, allostery, structure modelling
- Jan Paleček
- Protein interactions - domains, surface - bond types - interactome (maps, evolution) - protein complexes - principles of assembly, modules - molecular machines.
- David Potěšil
- Bioinformatics and proteins - Mw, pI, primary structure, PTMs, domains, tertiary structure, gene ontology (GO), phylogenetic similarity (mutations, proteins from organisms with unsequenced genomes), protein complexes.
- Zbyněk Zdráhal
- Importance and utilisation of proteomics - role of proteomics in basic research, application of proteomics (disease diagnostics, pathogene identification)
- Literature
- Teaching methods
- the lecture is based on ppt presentations and their explication. presentations themselves will be available as study material. it is recommended to attend the lecture, because of the explication, which significantly extends the presentations, and because of the limited availability of textbooks in english covering certain parts of the subject.
- Assessment methods
- the basic written examination takes 90 minutes and consists of a single-choice test with sixty questions, five choices per question. to pass the test, it is necessary to answer correctly at least 60 % of the questions; the test covers the complete content of the course. the examination will conclude with an oral examination.
during the course, students will be given ungraded, voluntary, time-saving tasks to consolidate the acquired knowledge. - Language of instruction
- Czech
- Further comments (probably available only in Czech)
- Study Materials
The course is taught annually. - Listed among pre-requisites of other courses
- Teacher's information
- 21., 28. 9. a 5. 10. 2020 - jan havliš 12. 10. a 19. 10. 2020 - tomáš klumpler 26. 10. a 2. 11. 2020 - honza paleček 9. 11. a 16. 11. 2020 - david potěšil 23. 11. 2020 - zbyněk dráhal
CG010 Proteomics
Faculty of ScienceAutumn 2020
- Extent and Intensity
- 2/0/0. 2 credit(s) (plus 2 credits for an exam). Type of Completion: zk (examination).
- Teacher(s)
- doc. Mgr. Jan Havliš, Dr. (lecturer)
prof. RNDr. Zbyněk Zdráhal, Dr. (lecturer)
Mgr. David Potěšil, Ph.D. (lecturer)
Mgr. Tomáš Klumpler, Ph.D. (lecturer)
doc. Mgr. Jan Paleček, Dr. rer. nat. (lecturer) - Guaranteed by
- doc. Mgr. Jan Havliš, Dr.
National Centre for Biomolecular Research – Faculty of Science
Supplier department: National Centre for Biomolecular Research – Faculty of Science - Timetable
- Tue 9:00–10:50 C02/211
- Prerequisites
- basics in biochemistry, analytical and physical chemistry
- Course Enrolment Limitations
- The course is also offered to the students of the fields other than those the course is directly associated with.
- fields of study / plans the course is directly associated with
- Genomics and Proteomics (programme PřF, N-BCH)
- Course objectives
- major goal of this subject is to acquaint students overall and generally with proteomics as a field, with its content and main aspects.
- Learning outcomes
- at the end of the course students should be able:
to understand and to explain terms related to proteomics (protein biosynthesis, sequence, structure and interactions);
to know relations between protein properties and methods of their study
to use this knowledge on proteins and their complexes to follow their role in organisms. - Syllabus
- Jan Havliš
- Introduction into proteomics – definition of proteome and proteomics. Why it is so important to study proteome and its changes: postgenomic era and what to do with information, which we cannot read, genotype vs. phenotype, what does happen during expression, from gene to protein and back. Approaches of contemporary proteomics: Expression, purification and analysis of recombinant proteins, analysis of relations between structure and function, differential proteomics, analysis of post-translational modifications
- Proteins - biosynthesis of proteins, basic structure hierarchy, basic protein properties (size and shape, polarity, charge, reactivity). Expression proteomics - the conditions and regulation of gene products expression (under different conditions, also ontogenically), protein identity: protoprotein, protein splicing (intein, extein), post-translational modifications, transport, localisation of proteins (eg. cell membrane proteins, secretome), degradation, relations between genotype and phenotype.
- Tomáš Klumpler
- structural proteomics - domains, tertiary structure, protein folding, structure and environment relations, allostery, structure modelling
- Jan Paleček
- Protein interactions - domains, surface - bond types - interactome (maps, evolution) - protein complexes - principles of assembly, modules - molecular machines.
- David Potěšil
- Bioinformatics and proteins - Mw, pI, primary structure, PTMs, domains, tertiary structure, gene ontology (GO), phylogenetic similarity (mutations, proteins from organisms with unsequenced genomes), protein complexes.
- Zbyněk Zdráhal
- Importance and utilisation of proteomics - role of proteomics in basic research, application of proteomics (disease diagnostics, pathogene identification)
- Literature
- Teaching methods
- the lecture, either offline or online, is based on ppt presentations and their explication. presentations them-selves will be available as a study material. it is recommended to attend the lecture, because of the explication, which significantly extends the presentations and because of limited availability of textbooks in english covering certain parts of the subject.
- Assessment methods
- basic written examination takes 90 minutes and consists of single-choice test with sixty questions, five choices per question. to pass the test, it is necessary to answer correctly at least 60 % of the questions; test covers the complete content of the course. the examination will conclude with an oral examination.
during the course, students will be given ungraded, voluntary, time-saving tasks to consolidate the acquired knowledge. - Language of instruction
- Czech
- Further comments (probably available only in Czech)
- Study Materials
The course is taught annually. - Listed among pre-requisites of other courses
- Teacher's information
- videocon lectures will take place in the MS teams environment. if possible, download the environment application. all MU students have access to it via office 365, see "external services" in IS. i recommend learning to work with the application in advance. the use of a browser version restricts your access to some useful functions. the lecture will be recorded in mp4 format and then uploaded in the study materials in IS. MS teams guides: https://is.muni.cz/auth/do/mu/samostudium/pages_en/02-online.html 06., 13. a 20. 10. 2020 - moje maličkost 27. 10. a 03. 11. 2020 - tomáš klumpler 10. 11. a 24. 11. 2020 - honza paleček 01 12. a 08. 12. 2020 - david potěšil 15. 12. 2020 - zbyněk dráhal
CG010 Proteomics
Faculty of ScienceAutumn 2019
- Extent and Intensity
- 2/0/0. 2 credit(s) (plus 2 credits for an exam). Type of Completion: zk (examination).
- Teacher(s)
- doc. Mgr. Jan Havliš, Dr. (lecturer)
prof. RNDr. Zbyněk Zdráhal, Dr. (lecturer)
Mgr. David Potěšil, Ph.D. (lecturer)
Mgr. Tomáš Klumpler, Ph.D. (lecturer)
doc. Mgr. Jan Paleček, Dr. rer. nat. (lecturer) - Guaranteed by
- doc. Mgr. Jan Havliš, Dr.
National Centre for Biomolecular Research – Faculty of Science
Supplier department: National Centre for Biomolecular Research – Faculty of Science - Timetable
- Tue 9:00–10:50 C02/211
- Prerequisites
- basics in biochemistry, analytical and physical chemistry
- Course Enrolment Limitations
- The course is also offered to the students of the fields other than those the course is directly associated with.
- fields of study / plans the course is directly associated with
- Genomics and Proteomics (programme PřF, N-BCH)
- Course objectives
- major goal of this subject is to acquaint students overall and generally with proteomics as a field, with its content and main aspects.
- Learning outcomes
- at the end of the course students should be able:
to understand and to explain terms related to proteomics (protein biosynthesis, sequence, structure and interactions);
to know relations between protein properties and methods of their study
to use this knowledge on proteins and their complexes to follow their role in organisms. - Syllabus
- Jan Havliš
- Introduction into proteomics – definition of proteome and proteomics. Why it is so important to study proteome and its changes: postgenomic era and what to do with information, which we cannot read, genotype vs. phenotype, what does happen during expression, from gene to protein and back. Approaches of contemporary proteomics: Expression, purification and analysis of recombinant proteins, analysis of relations between structure and function, differential proteomics, analysis of post-translational modifications
- Proteins - biosynthesis of proteins, basic structure hierarchy, basic protein properties (size and shape, polarity, charge, reactivity). Expression proteomics - the conditions and regulation of gene products expression (under different conditions, also ontogenically), protein identity: protoprotein, protein splicing (intein, extein), post-translational modifications, transport, localisation of proteins (eg. cell membrane proteins, secretome), degradation, relations between genotype and phenotype.
- Tomáš Klumpler
- structural proteomics - domains, tertiary structure, protein folding, structure and environment relations, allostery, structure modelling
- Jan Paleček
- Protein interactions - domains, surface - bond types - interactome (maps, evolution) - protein complexes - principles of assembly, modules - molecular machines.
- David Potěšil
- Bioinformatics and proteins - Mw, pI, primary structure, PTMs, domains, tertiary structure, gene ontology (GO), phylogenetic similarity (mutations, proteins from organisms with unsequenced genomes), protein complexes.
- Zbyněk Zdráhal
- Importance and utilisation of proteomics - role of proteomics in basic research, application of proteomics (disease diagnostics, pathogene identification)
- Literature
- Teaching methods
- The lecture is based on ppt presentations and their explication. Presentations themselves will be available as study materials (black-and-white printable pdf with high resolution and restricted access rights). It is recommended to attend the lecture, because of the explication, which significantly extends the presentation and because there are no available textbooks in Czech language covering certain parts of the subject. Students will test their acquired knowledge by means of "in-rough" tests, which will have similar form and content as the final examination test, they will be corrected to give the feed-back, but not graded.
- Assessment methods
- written & oral examination; single-choice test consists of sixty questions with five choices per question. to pass the test, it is necessary to answer correctly at least 60 % of the questions; test covers complete content of the course. the examination will be finished by oral examination.
- Language of instruction
- Czech
- Further Comments
- Study Materials
The course is taught annually. - Listed among pre-requisites of other courses
CG010 Proteomics
Faculty of ScienceAutumn 2018
- Extent and Intensity
- 2/0/0. 2 credit(s) (plus 2 credits for an exam). Type of Completion: zk (examination).
- Teacher(s)
- doc. Mgr. Jan Havliš, Dr. (lecturer)
prof. RNDr. Zbyněk Zdráhal, Dr. (lecturer)
Mgr. David Potěšil, Ph.D. (lecturer)
Mgr. Tomáš Klumpler, Ph.D. (lecturer)
doc. Mgr. Jan Paleček, Dr. rer. nat. (lecturer) - Guaranteed by
- prof. RNDr. Jiří Fajkus, CSc.
National Centre for Biomolecular Research – Faculty of Science
Supplier department: National Centre for Biomolecular Research – Faculty of Science - Timetable
- Mon 17. 9. to Fri 14. 12. Tue 9:00–10:50 C02/211
- Prerequisites
- basics in biochemistry, analytical and physical chemistry
- Course Enrolment Limitations
- The course is also offered to the students of the fields other than those the course is directly associated with.
- fields of study / plans the course is directly associated with
- Genomics and Proteomics (programme PřF, N-BCH)
- Course objectives
- major goal of this subject is to acquaint students overall and generally with proteomics as a field, with its content and main aspects.
- Learning outcomes
- at the end of the course students should be able:
to understand and to explain terms related to proteomics (protein biosynthesis, sequence, structure and interactions);
to know relations between protein properties and methods of their study
to use this knowledge on proteins and their complexes to follow their role in organisms. - Syllabus
- Jan Havliš
- Introduction into proteomics – definition of proteome and proteomics. Why it is so important to study proteome and its changes: postgenomic era and what to do with information, which we cannot read, genotype vs. phenotype, what does happen during expression, from gene to protein and back. Approaches of contemporary proteomics: Expression, purification and analysis of recombinant proteins, analysis of relations between structure and function, differential proteomics, analysis of post-translational modifications
- Proteins - biosynthesis of proteins, basic structure hierarchy, basic protein properties (size and shape, polarity, charge, reactivity). Expression proteomics - the conditions and regulation of gene products expression (under different conditions, also ontogenically), protein identity: protoprotein, protein splicing (intein, extein), post-translational modifications, transport, localisation of proteins (eg. cell membrane proteins, secretome), degradation, relations between genotype and phenotype.
- Tomáš Klumpler
- structural proteomics - domains, tertiary structure, protein folding, structure and environment relations, allostery, structure modelling
- Jan Paleček
- Protein interactions - domains, surface - bond types - interactome (maps, evolution) - protein complexes - principles of assembly, modules - molecular machines.
- David Potěšil
- Bioinformatics and proteins - Mw, pI, primary structure, PTMs, domains, tertiary structure, gene ontology (GO), phylogenetic similarity (mutations, proteins from organisms with unsequenced genomes), protein complexes.
- Zbyněk Zdráhal
- Importance and utilisation of proteomics - role of proteomics in basic research, application of proteomics (disease diagnostics, pathogene identification)
- Literature
- Teaching methods
- The lecture is based on ppt presentations and their explication. Presentations themselves will be available as study materials (black-and-white printable pdf with high resolution and restricted access rights). It is recommended to attend the lecture, because of the explication, which significantly extends the presentation and because there are no available textbooks in Czech language covering certain parts of the subject. Students will test their acquired knowledge by means of "in-rough" tests, which will have similar form and content as the final examination test, they will be corrected to give the feed-back, but not graded.
- Assessment methods
- written & oral examination; single-choice test consists of sixty questions with five choices per question. to pass the test, it is necessary to answer correctly at least 60 % of the questions; test covers complete content of the course. the examination will be finished by oral examination.
- Language of instruction
- Czech
- Further Comments
- Study Materials
The course is taught annually. - Listed among pre-requisites of other courses
CG010 Proteomics
Faculty of Scienceautumn 2017
- Extent and Intensity
- 2/0/0. 2 credit(s) (plus 2 credits for an exam). Type of Completion: zk (examination).
- Teacher(s)
- doc. Mgr. Jan Havliš, Dr. (lecturer)
prof. RNDr. Zbyněk Zdráhal, Dr. (lecturer)
Mgr. David Potěšil, Ph.D. (lecturer)
Mgr. Tomáš Klumpler, Ph.D. (lecturer)
doc. Mgr. Jan Paleček, Dr. rer. nat. (lecturer) - Guaranteed by
- prof. RNDr. Jiří Fajkus, CSc.
National Centre for Biomolecular Research – Faculty of Science
Supplier department: National Centre for Biomolecular Research – Faculty of Science - Timetable
- Mon 18. 9. to Fri 15. 12. Tue 9:00–10:50 C02/211
- Prerequisites
- basics in biochemistry, analytical and physical chemistry
- Course Enrolment Limitations
- The course is also offered to the students of the fields other than those the course is directly associated with.
- fields of study / plans the course is directly associated with
- Genomics and Proteomics (programme PřF, N-BCH)
- Course objectives
- major goal of this subject is to acquaint students overall and generally with proteomics as a field, with its content and main aspects.
- Learning outcomes
- at the end of the course students should be able:
to understand and to explain terms related to proteomics (protein biosynthesis, sequence, structure and interactions);
to know relations between protein properties and methods of their study
to use this knowledge on proteins and their complexes to follow their role in organisms. - Syllabus
- Jan Havliš
- Introduction into proteomics – definition of proteome and proteomics. Why it is so important to study proteome and its changes: postgenomic era and what to do with information, which we cannot read, genotype vs. phenotype, what does happen during expression, from gene to protein and back. Approaches of contemporary proteomics: Expression, purification and analysis of recombinant proteins, analysis of relations between structure and function, differential proteomics, analysis of post-translational modifications
- Proteins - biosynthesis of proteins, basic structure hierarchy, basic protein properties (size and shape, polarity, charge, reactivity). Expression proteomics - the conditions and regulation of gene products expression (under different conditions, also ontogenically), protein identity: protoprotein, protein splicing (intein, extein), post-translational modifications, transport, localisation of proteins (eg. cell membrane proteins, secretome), degradation, relations between genotype and phenotype.
- Tomáš Klumpler
- structural proteomics - domains, tertiary structure, protein folding, structure and environment relations, allostery, structure modelling
- Jan Paleček
- Protein interactions - domains, surface - bond types - interactome (maps, evolution) - protein complexes - simple (dimers), multicomponential (SMC...), molecular machinery.
- David Potěšil
- Bioinformatics and proteins - Mw, pI, primary structure, PTMs, domains, tertiary structure, gene ontology (GO), phylogenetic similarity (mutations, proteins from organisms with unsequenced genomes), protein complexes.
- Zbyněk Zdráhal
- Importance and utilisation of proteomics - role of proteomics in basic research, application of proteomics (disease diagnostics, pathogene identification)
- Literature
- Teaching methods
- The lecture is based on ppt presentations and their explication. Presentations themselves will be available as study materials (black-and-white printable pdf with high resolution and restricted access rights). It is recommended to attend the lecture, because of the explication, which significantly extends the presentation and because there are no available textbooks in Czech language covering certain parts of the subject. Students will test their acquired knowledge by means of "in-rough" tests, which will have similar form and content as the final examination test, they will be corrected to give the feed-back, but not graded.
- Assessment methods
- written & oral examination; single-choice test consists of sixty questions with five choices per question. to pass the test, it is necessary to answer correctly at least 60 % of the questions; test covers complete content of the course. the examination will be finished by oral examination.
- Language of instruction
- Czech
- Further Comments
- Study Materials
The course is taught annually. - Listed among pre-requisites of other courses
CG010 Proteomics
Faculty of ScienceAutumn 2016
- Extent and Intensity
- 2/0/0. 2 credit(s) (plus 2 credits for an exam). Type of Completion: zk (examination).
- Teacher(s)
- doc. Mgr. Jan Havliš, Dr. (lecturer)
prof. RNDr. Zbyněk Zdráhal, Dr. (lecturer)
Mgr. David Potěšil, Ph.D. (lecturer)
Mgr. Tomáš Klumpler, Ph.D. (lecturer)
doc. Mgr. Jan Paleček, Dr. rer. nat. (lecturer) - Guaranteed by
- prof. RNDr. Jiří Fajkus, CSc.
National Centre for Biomolecular Research – Faculty of Science
Supplier department: National Centre for Biomolecular Research – Faculty of Science - Timetable
- Mon 19. 9. to Sun 18. 12. Tue 9:00–10:50 C02/211
- Prerequisites
- basics in biochemistry, analytical and physical chemistry
- Course Enrolment Limitations
- The course is also offered to the students of the fields other than those the course is directly associated with.
- fields of study / plans the course is directly associated with
- Genomics and Proteomics (programme PřF, N-BCH)
- Course objectives
- At the end of the course students should be able: to understand and to explain terms related to proteomics (protein biosynthesis, sequence, structure and interactions); to know relations between protein properties and methods of their study, to be able to use this knowledge on proteins and their complexes to follow their role in organisms.
- Syllabus
- Jan Havliš
- Introduction into proteomics – definition of proteome and proteomics. Why it is so important to study proteome and its changes: postgenomic era and what to do with information, which we cannot read, genotype vs. phenotype, what does happen during expression, from gene to protein and back. Approaches of contemporary proteomics: Expression, purification and analysis of recombinant proteins, analysis of relations between structure and function, differential proteomics, analysis of post-translational modifications
- Proteins - biosynthesis of proteins, basic structure hierarchy, basic protein properties (size and shape, polarity, charge, reactivity). Expression proteomics - the conditions and regulation of gene products expression (under different conditions, also ontogenically), protein identity: protoprotein, protein splicing (intein, extein), post-translational modifications, transport, localisation of proteins (eg. cell membrane proteins, secretome), degradation, relations between genotype and phenotype.
- Tomáš Klumpler
- structural proteomics - domains, tertiary structure, protein folding, structure and environment relations, allostery, structure modelling
- Jan Paleček
- Protein interactions - domains, surface - bond types - interactome (maps, evolution) - protein complexes - simple (dimers), multicomponential (SMC...), molecular machinery.
- David Potěšil
- Bioinformatics and proteins - Mw, pI, primary structure, PTMs, domains, tertiary structure, gene ontology (GO), phylogenetic similarity (mutations, proteins from organisms with unsequenced genomes), protein complexes.
- Zbyněk Zdráhal
- Importance and utilisation of proteomics - role of proteomics in basic research, application of proteomics (disease diagnostics, pathogene identification)
- Literature
- Teaching methods
- The lecture is based on ppt presentations and their explication. Presentations themselves will be available as study materials (black-and-white printable pdf with high resolution and restricted access rights). It is recommended to attend the lecture, because of the explication, which significantly extends the presentation and because there are no available textbooks in Czech language covering certain parts of the subject.
- Assessment methods
- written examination; single-choice test consists of sixty questions with four choices per question. to pass the subject, it is necessary to answer correctly at least 60 % of the questions. test covers complete content of the course.
- Language of instruction
- Czech
- Further Comments
- Study Materials
The course is taught annually. - Listed among pre-requisites of other courses
CG010 Proteomics
Faculty of ScienceAutumn 2015
- Extent and Intensity
- 2/0/0. 2 credit(s) (plus 2 credits for an exam). Type of Completion: zk (examination).
- Teacher(s)
- doc. Mgr. Jan Havliš, Dr. (lecturer)
prof. RNDr. Zbyněk Zdráhal, Dr. (lecturer)
Mgr. David Potěšil, Ph.D. (lecturer)
doc. RNDr. Jaromír Marek, Ph.D. (lecturer)
doc. Mgr. Jan Paleček, Dr. rer. nat. (lecturer)
Mgr. Pavla Pospíšilová (assistant)
Mgr. Jan Škoda (assistant) - Guaranteed by
- prof. RNDr. Jiří Fajkus, CSc.
National Centre for Biomolecular Research – Faculty of Science
Supplier department: National Centre for Biomolecular Research – Faculty of Science - Timetable
- Tue 9:00–10:50 C02/211
- Prerequisites
- basics in biochemistry, analytical and physical chemistry
- Course Enrolment Limitations
- The course is also offered to the students of the fields other than those the course is directly associated with.
- fields of study / plans the course is directly associated with
- Genomics and Proteomics (programme PřF, N-BCH)
- Course objectives
- At the end of the course students should be able: to understand and to explain terms related to proteomics (protein biosynthesis, sequence, structure and interactions); to know relations between protein properties and methods of their study, to be able to use this knowledge on proteins and their complexes to follow their role in organisms.
- Syllabus
- Jan Havliš
- Introduction into proteomics – definition of proteome and proteomics. Why it is so important to study proteome and its changes: postgenomic era and what to do with information, which we cannot read, genotype vs. phenotype, what does happen during expression, from gene to protein and back. Approaches of contemporary proteomics: Expression, purification and analysis of recombinant proteins, analysis of relations between structure and function, differential proteomics, analysis of post-translational modifications
- Proteins - biosynthesis of proteins, basic structure hierarchy, basic protein properties (size and shape, polarity, charge, reactivity). Expression proteomics - the conditions and regulation of gene products expression (under different conditions, also ontogenically), protein identity: protoprotein, protein splicing (intein, extein), post-translational modifications, transport, localisation of proteins (eg. cell membrane proteins, secretome), degradation, relations between genotype and phenotype.
- Jaromír Marek
- structural proteomics - domains, tertiary structure, protein folding, structure and environment relations, allostery, structure modelling
- Jan Paleček
- Protein interactions - domains, surface - bond types - interactome (maps, evolution) - protein complexes - simple (dimers), multicomponential (SMC...), molecular machinery.
- Zbyněk Zdráhal
- Bioinformatics and proteins - Mw, pI, primary structure, PTMs, domains, tertiary structure, gene ontology (GO), phylogenetic similarity (mutations, proteins from organisms with unsequenced genomes), protein complexes.
- Zbyněk Zdráhal
- Importance and utilisation of proteomics - role of proteomics in basic research, application of proteomics (disease diagnostics, pathogene identification)
- Literature
- Teaching methods
- The lecture is based on ppt presentations and their explication. Presentations themselves will be available as study materials (black-and-white printable pdf with high resolution and restricted access rights). It is recommended to attend the lecture, because of the explication, which significantly extends the presentation and because there are no available textbooks in Czech language covering certain parts of the subject.
- Assessment methods
- Oral examination; students are required to understand and to be familiar with the principles and its applications. Examination consists of three basic questions, which would be during the examination expanded to let the student demonstrate the extent of topic understanding.
- Language of instruction
- Czech
- Further Comments
- Study Materials
The course is taught annually. - Listed among pre-requisites of other courses
CG010 Proteomics
Faculty of ScienceAutumn 2014
- Extent and Intensity
- 2/0. 2 credit(s) (plus 2 credits for an exam). Type of Completion: zk (examination).
- Teacher(s)
- doc. Mgr. Jan Havliš, Dr. (lecturer)
prof. RNDr. Zbyněk Zdráhal, Dr. (lecturer)
Mgr. David Potěšil, Ph.D. (lecturer)
doc. RNDr. Jaromír Marek, Ph.D. (lecturer)
doc. Mgr. Jan Paleček, Dr. rer. nat. (lecturer) - Guaranteed by
- prof. RNDr. Zdeněk Glatz, CSc.
National Centre for Biomolecular Research – Faculty of Science
Supplier department: National Centre for Biomolecular Research – Faculty of Science - Timetable
- Tue 8:00–9:50 C02/211
- Prerequisites
- basics in biochemistry, analytical and physical chemistry
- Course Enrolment Limitations
- The course is also offered to the students of the fields other than those the course is directly associated with.
- fields of study / plans the course is directly associated with
- Genomics and Proteomics (programme PřF, N-BCH)
- Course objectives
- At the end of the course students should be able: to understand and to explain terms related to proteomics (protein biosynthesis, sequence, structure and interactions); to know relations between protein properties and methods of their study, to be able to use this knowledge on proteins and their complexes to follow their role in organisms.
- Syllabus
- Jan Havliš
- Introduction into proteomics – definition of proteome and proteomics. Why it is so important to study proteome and its changes: postgenomic era and what to do with information, which we cannot read, genotype vs. phenotype, what does happen during expression, from gene to protein and back. Approaches of contemporary proteomics: Expression, purification and analysis of recombinant proteins, analysis of relations between structure and function, differential proteomics, analysis of post-translational modifications
- Proteins - biosynthesis of proteins, basic structure hierarchy, basic protein properties (size and shape, polarity, charge, reactivity). Expression proteomics - the conditions and regulation of gene products expression (under different conditions, also ontogenically), protein identity: protoprotein, protein splicing (intein, extein), post-translational modifications, transport, localisation of proteins (eg. cell membrane proteins, secretome), degradation, relations between genotype and phenotype.
- Jaromír Marek
- structural proteomics - domains, tertiary structure, protein folding, structure and environment relations, allostery, structure modelling
- Jan Paleček
- Protein interactions - domains, surface - bond types - interactome (maps, evolution) - protein complexes - simple (dimers), multicomponential (SMC...), molecular machinery.
- Zbyněk Zdráhal
- Bioinformatics and proteins - Mw, pI, primary structure, PTMs, domains, tertiary structure, gene ontology (GO), phylogenetic similarity (mutations, proteins from organisms with unsequenced genomes), protein complexes.
- Zbyněk Zdráhal
- Importance and utilisation of proteomics - role of proteomics in basic research, application of proteomics (disease diagnostics, pathogene identification)
- Literature
- Teaching methods
- The lecture is based on ppt presentations and their explication. Presentations themselves will be available as study materials (black-and-white printable pdf with high resolution and restricted access rights). It is recommended to attend the lecture, because of the explication, which significantly extends the presentation and because there are no available textbooks in Czech language covering certain parts of the subject.
- Assessment methods
- Oral examination; students are required to understand and to be familiar with the principles and its applications. Examination consists of three basic questions, which would be during the examination expanded to let the student demonstrate the extent of topic understanding.
- Language of instruction
- Czech
- Further Comments
- Study Materials
The course is taught annually. - Listed among pre-requisites of other courses
CG010 Proteomics
Faculty of ScienceAutumn 2013
- Extent and Intensity
- 2/0. 2 credit(s) (plus 2 credits for an exam). Type of Completion: zk (examination).
- Teacher(s)
- doc. Mgr. Jan Havliš, Dr. (lecturer)
prof. RNDr. Zbyněk Zdráhal, Dr. (lecturer)
doc. RNDr. Jan Hejátko, Ph.D. (lecturer), prof. RNDr. Jiří Fajkus, CSc. (deputy)
doc. RNDr. Jaromír Marek, Ph.D. (lecturer)
doc. Mgr. Jan Paleček, Dr. rer. nat. (lecturer) - Guaranteed by
- prof. RNDr. Zdeněk Glatz, CSc.
Department of Biochemistry – Chemistry Section – Faculty of Science
Supplier department: National Centre for Biomolecular Research – Faculty of Science - Timetable
- Mon 10:00–11:50 C02/211
- Prerequisites
- basics in biochemistry, analytical and physical chemistry
- Course Enrolment Limitations
- The course is also offered to the students of the fields other than those the course is directly associated with.
- fields of study / plans the course is directly associated with
- Genomics and Proteomics (programme PřF, N-BCH)
- Course objectives
- At the end of the course students should be able: to understand and to explain terms related to proteomics (protein biosynthesis, sequence, structure and interactions); to know relations between protein properties and methods of their study, to be able to use this knowledge on proteins and their complexes to follow their role in organisms.
- Syllabus
- Jan Hejátko
- Introduction into proteomics – definition of proteome and proteomics. Why it is so important to study proteome and its changes: postgenomic era and what to do with information, which we cannot read, genotype vs. phenotype, what does happen during expression, from gene to protein and back. Approaches of contemporary proteomics: Expression, purification and analysis of recombinant proteins, analysis of relations between structure and function, differential proteomics, analysis of post-translational modifications
- Jan Havliš
- Proteins - biosynthesis of proteins, basic structure hierarchy, basic protein properties (size and shape, polarity, charge, reactivity). Expression proteomics - the conditions and regulation of gene products expression (under different conditions, also ontogenically), protein identity: protoprotein, protein splicing (intein, extein), post-translational modifications, transport, localisation of proteins (eg. cell membrane proteins, secretome), degradation, relations between genotype and phenotype.
- Jaromír Marek
- structural proteomics - domains, tertiary structure, protein folding, structure and environment relations, allostery, structure modelling
- Jan Paleček
- Protein interactions - domains, surface - bond types - interactome (maps, evolution) - protein complexes - simple (dimers), multicomponential (SMC...), molecular machinery.
- Zbyněk Zdráhal
- Bioinformatics and proteins - Mw, pI, primary structure, PTMs, domains, tertiary structure, gene ontology (GO), phylogenetic similarity (mutations, proteins from organisms with unsequenced genomes), protein complexes.
- Zbyněk Zdráhal
- Importance and utilisation of proteomics - role of proteomics in basic research, application of proteomics (disease diagnostics, pathogene identification)
- Literature
- Teaching methods
- The lecture is based on ppt presentations and their explication. Presentations themselves will be available as study materials (black-and-white printable pdf with high resolution and restricted access rights). It is recommended to attend the lecture, because of the explication, which significantly extends the presentation and because there are no available textbooks in Czech language covering certain parts of the subject.
- Assessment methods
- Oral examination; students are required to understand and to be familiar with the principles and its applications. Examination consists of three basic questions, which would be during the examination expanded to let the student demonstrate the extent of topic understanding.
- Language of instruction
- Czech
- Further Comments
- Study Materials
The course is taught annually. - Listed among pre-requisites of other courses
CG010 Proteomics
Faculty of ScienceAutumn 2012
- Extent and Intensity
- 2/0. 2 credit(s) (plus 2 credits for an exam). Type of Completion: zk (examination).
- Teacher(s)
- doc. Mgr. Jan Havliš, Dr. (lecturer)
prof. RNDr. Zbyněk Zdráhal, Dr. (lecturer)
doc. RNDr. Jan Hejátko, Ph.D. (lecturer), prof. RNDr. Jiří Fajkus, CSc. (deputy)
doc. RNDr. Jaromír Marek, Ph.D. (lecturer)
doc. Mgr. Jan Paleček, Dr. rer. nat. (lecturer) - Guaranteed by
- doc. Mgr. Jan Havliš, Dr.
Department of Biochemistry – Chemistry Section – Faculty of Science
Supplier department: Department of Biochemistry – Chemistry Section – Faculty of Science - Timetable
- Tue 11:00–12:50 C02/211
- Prerequisites
- basics in biochemistry, analytical and physical chemistry
- Course Enrolment Limitations
- The course is also offered to the students of the fields other than those the course is directly associated with.
- fields of study / plans the course is directly associated with
- Genomics and Proteomics (programme PřF, D-BI4)
- Genomics and Proteomics (programme PřF, N-BCH)
- Course objectives
- at the end of the course students should be able to: to understand and to explain terms related to proteomics (protein biosynthesis, sequence, structure and interactions); to know relations between between protein properties and methods of their study, to be able to use this knowledge on proteins and their complexes to follow their role in organisms.
- Syllabus
- Jan Hejátko
- Introduction into proteomics – definition of proteome and proteomics. Why it is so important to study proteome and its changes: postgenimic era and what to do with inofmration, which we cannot read, genotype vs. phenotype, what does happen during expression, from gene to protein and back. Approaches of contemporary proteomics: Expression, purification and analysis of recombinant proteins, analysis of relations between structure and function, differential proteomics, analysis of post-translation modifications
- Jan Havliš
- Proteins - biosynthesis of proteins, basic structure hierarchy, basic protein properties (size and shape, polarity, charge, reactivity). Expression proteomics - the conditions and regulation of gene products expression (under different conditions, also ontogenically), protein identity: protoprotein, protein splicing (intein, extein), post-translational modifications, transport, localisation of proteins (eg. cell membrane proteins, secretome), degradation, relations between genotype and phenotype.
- Jaromír Marek
- structural proteomics - domains, tertiary structure, protein folding, structure and environment relations, allostery, structure modelling
- Jan Paleček
- Protein interactions - domains, surface - bond types - interactome (maps, evolution) - protein complexes - simple (dimers), multicomponential (SMC...), molekular machinery.
- Zbyněk Zdráhal
- Bioinformatics and proteins - Mw, pI, primary structure, PTMs, domains, tertiary structure, gene ontology (GO), phylogenetic similarity (mutations, proteins from organisms with unsequences genomes), protein complexes.
- Zbyněk Zdráhal
- Importance and utilisation of proteomics - role of proteomics in basic research, application of proteomics (disease diagnostics, pathogene identification)
- Literature
- Teaching methods
- the lecture is based on ppt presentations and their explication. presentations them-self will be available as study materials (black-and-white printable pdf with high resolution and restricted access rights). it is recommended to attend the lecture, because of the explication, which significantly extends the presentation and because there are no available textbooks in czech language covering certain parts of the subject.
- Assessment methods
- oral examination; students are required to understand and be familiar with the principles and its applications. examination consists of three basic questions, which would be during the examination expanded to let the student demonstrate the extent of topic understanding
- Language of instruction
- Czech
- Further Comments
- Study Materials
The course is taught annually. - Listed among pre-requisites of other courses
CG010 Proteomics
Faculty of ScienceAutumn 2011
The course is not taught in Autumn 2011
- Extent and Intensity
- 2/0. 2 credit(s) (plus 2 credits for an exam). Type of Completion: zk (examination).
- Teacher(s)
- doc. Mgr. Jan Havliš, Dr. (lecturer)
prof. RNDr. Zbyněk Zdráhal, Dr. (lecturer)
doc. RNDr. Jan Hejátko, Ph.D. (lecturer)
doc. RNDr. Jaromír Marek, Ph.D. (lecturer) - Guaranteed by
- doc. Mgr. Jan Havliš, Dr.
Department of Biochemistry – Chemistry Section – Faculty of Science - Prerequisites
- basics in biochemistry, analytical and physical chemistry
- Course Enrolment Limitations
- The course is also offered to the students of the fields other than those the course is directly associated with.
- fields of study / plans the course is directly associated with
- Genomics and Proteomics (programme PřF, D-BI4)
- Course objectives
- at the end of the course students should be able to: understand and explain terms related to proteomics; work with information on proteins and their complexes to follow their role in systems biology;
- Syllabus
- Jan Hejátko
- inroduction into proteomics – definition of proteome (dynamic p.), relations between genomics and proteomics, proteosynthesis and the basic hierarchy of protein structure, protein properties (size and shape, polarity, charge, reactivity))
- Jan Havliš
- expression proteomics - the conditions and regulation of gene products expression (under different conditions, also ontogenically) protein identity: protoprotein, protein splicing (intein, extein), post-translational modifications, transport, localisation of proteins (eg. cell membrane proteins, secretome), degradation, relations between genotype and phenotype
- Jaromír Marek
- structural proteomics - domains, tertiary structure, protein folding, structure and environment relations, allostery, structure modelling
- Jan Paleček
- functional proteomics - the role of proteins (enzymes, signalling molecules, transport molecules, structural molecules), relations between structure and function (domains, protein complexes), relations between localisation and function (interactive maps), relations between the content (and form) of protein and its function, interaction with aprotic molecules
- Zbyněk Zdráhal
- bioinformatics and proteins - Mw, pI, primary structure, PTMs, domains, tertiary structure, protein complexes, gene ontology (GO); phylogenetic similarity, the effect of mutations on the structure and function
- Zbyněk Zdráhal
- importance and use of proteomics - the contextual analytical proteomics, diagnostic proteomics (biomarkers), single cell proteomics, proteomic aspects of systems biology
- Literature
- Teaching methods
- the lecture is based on ppt presentations and their explication. presentations them-self will be available as study materials (black-and-white printable pdf with high resolution and restricted access rights). it is recommended to attend the lecture, because of the explication, which significantly extends the presentation and because there are no available textbooks in czech language covering certain parts of the subject.
- Assessment methods
- oral examination; students are required to understand and be familiar with the principles and its applications. examination consists of three basic questions, which would be during the examination expanded to let the student demonstrate the extent of topic understanding
- Language of instruction
- Czech
- Further Comments
- The course is taught annually.
The course is taught: every week. - Listed among pre-requisites of other courses
CG010 Proteomics
Faculty of ScienceAutumn 2010
The course is not taught in Autumn 2010
- Extent and Intensity
- 2/0. 2 credit(s) (plus 2 credits for an exam). Type of Completion: zk (examination).
- Teacher(s)
- doc. Mgr. Jan Havliš, Dr. (lecturer)
prof. RNDr. Zbyněk Zdráhal, Dr. (lecturer)
doc. RNDr. Jan Hejátko, Ph.D. (lecturer)
doc. RNDr. Jaromír Marek, Ph.D. (lecturer) - Guaranteed by
- doc. Mgr. Jan Havliš, Dr.
Department of Biochemistry – Chemistry Section – Faculty of Science - Prerequisites
- basics in biochemistry, analytical and physical chemistry
- Course Enrolment Limitations
- The course is also offered to the students of the fields other than those the course is directly associated with.
- fields of study / plans the course is directly associated with
- Analytical Biochemistry (programme PřF, N-BCH)
- Biochemistry (programme PřF, N-BCH)
- Genomics and Proteomics (programme PřF, D-BI4)
- Course objectives
- at the end of the course students should be able to: understand and explain terms related to proteomics; work with information on proteins and their complexes to follow their role in systems biology;
- Syllabus
- Jan Hejátko
- inroduction into proteomics – definition of proteome (dynamic p.), relations between genomics and proteomics, proteosynthesis and the basic hierarchy of protein structure, protein properties (size and shape, polarity, charge, reactivity))
- Jan Havliš
- expression proteomics - the conditions and regulation of gene products expression (under different conditions, also ontogenically) protein identity: protoprotein, protein splicing (intein, extein), post-translational modifications, transport, localisation of proteins (eg. cell membrane proteins, secretome), degradation, relations between genotype and phenotype
- Jaromír Marek
- structural proteomics - domains, tertiary structure, protein folding, structure and environment relations, allostery, structure modelling
- Jan Paleček
- functional proteomics - the role of proteins (enzymes, signalling molecules, transport molecules, structural molecules), relations between structure and function (domains, protein complexes), relations between localisation and function (interactive maps), relations between the content (and form) of protein and its function, interaction with aprotic molecules
- Zbyněk Zdráhal
- bioinformatics and proteins - Mw, pI, primary structure, PTMs, domains, tertiary structure, protein complexes, gene ontology (GO); phylogenetic similarity, the effect of mutations on the structure and function
- Zbyněk Zdráhal
- importance and use of proteomics - the contextual analytical proteomics, diagnostic proteomics (biomarkers), single cell proteomics, proteomic aspects of systems biology
- Literature
- Teaching methods
- the lecture is based on ppt presentations and their explication. presentations them-self will be available as study materials (black-and-white printable pdf with high resolution and restricted access rights). it is recommended to attend the lecture, because of the explication, which significantly extends the presentation and because there are no available textbooks in czech language covering certain parts of the subject.
- Assessment methods
- oral examination; students are required to understand and be familiar with the principles and its applications. examination consists of three basic questions, which would be during the examination expanded to let the student demonstrate the extent of topic understanding
- Language of instruction
- Czech
- Further Comments
- The course is taught annually.
The course is taught: every week. - Listed among pre-requisites of other courses
CG010 Proteomics
Faculty of ScienceAutumn 2010 - only for the accreditation
- Extent and Intensity
- 2/0. 2 credit(s) (plus 2 credits for an exam). Type of Completion: zk (examination).
- Teacher(s)
- doc. Mgr. Jan Havliš, Dr. (lecturer)
prof. RNDr. Zbyněk Zdráhal, Dr. (lecturer)
doc. RNDr. Jan Hejátko, Ph.D. (lecturer)
doc. RNDr. Jaromír Marek, Ph.D. (lecturer) - Guaranteed by
- doc. Mgr. Jan Havliš, Dr.
Department of Biochemistry – Chemistry Section – Faculty of Science - Prerequisites
- basics in biochemistry, analytical and physical chemistry
- Course Enrolment Limitations
- The course is also offered to the students of the fields other than those the course is directly associated with.
- fields of study / plans the course is directly associated with
- Genomics and Proteomics (programme PřF, D-BI4)
- Course objectives
- at the end of the course students should be able to: understand and explain terms related to proteomics; work with information on proteins and their complexes to follow their role in systems biology;
- Syllabus
- Jan Hejátko
- inroduction into proteomics – definition of proteome (dynamic p.), relations between genomics and proteomics, proteosynthesis and the basic hierarchy of protein structure, protein properties (size and shape, polarity, charge, reactivity))
- Jan Havliš
- expression proteomics - the conditions and regulation of gene products expression (under different conditions, also ontogenically) protein identity: protoprotein, protein splicing (intein, extein), post-translational modifications, transport, localisation of proteins (eg. cell membrane proteins, secretome), degradation, relations between genotype and phenotype
- Jaromír Marek
- structural proteomics - domains, tertiary structure, protein folding, structure and environment relations, allostery, structure modelling
- Jan Paleček
- functional proteomics - the role of proteins (enzymes, signalling molecules, transport molecules, structural molecules), relations between structure and function (domains, protein complexes), relations between localisation and function (interactive maps), relations between the content (and form) of protein and its function, interaction with aprotic molecules
- Zbyněk Zdráhal
- bioinformatics and proteins - Mw, pI, primary structure, PTMs, domains, tertiary structure, protein complexes, gene ontology (GO); phylogenetic similarity, the effect of mutations on the structure and function
- Zbyněk Zdráhal
- importance and use of proteomics - the contextual analytical proteomics, diagnostic proteomics (biomarkers), single cell proteomics, proteomic aspects of systems biology
- Literature
- Teaching methods
- the lecture is based on ppt presentations and their explication. presentations them-self will be available as study materials (black-and-white printable pdf with high resolution and restricted access rights). it is recommended to attend the lecture, because of the explication, which significantly extends the presentation and because there are no available textbooks in czech language covering certain parts of the subject.
- Assessment methods
- oral examination; students are required to understand and be familiar with the principles and its applications. examination consists of three basic questions, which would be during the examination expanded to let the student demonstrate the extent of topic understanding
- Language of instruction
- Czech
- Further Comments
- The course is taught annually.
The course is taught: every week. - Listed among pre-requisites of other courses
CG010 Proteomics
Faculty of ScienceAutumn 2011 - acreditation
The course is not taught in Autumn 2011 - acreditation
The information about the term Autumn 2011 - acreditation is not made public
- Extent and Intensity
- 2/0. 2 credit(s) (plus 2 credits for an exam). Type of Completion: zk (examination).
- Teacher(s)
- doc. Mgr. Jan Havliš, Dr. (lecturer)
prof. RNDr. Zbyněk Zdráhal, Dr. (lecturer)
doc. RNDr. Jan Hejátko, Ph.D. (lecturer)
doc. RNDr. Jaromír Marek, Ph.D. (lecturer) - Guaranteed by
- doc. Mgr. Jan Havliš, Dr.
Department of Biochemistry – Chemistry Section – Faculty of Science - Prerequisites
- basics in biochemistry, analytical and physical chemistry
- Course Enrolment Limitations
- The course is also offered to the students of the fields other than those the course is directly associated with.
- fields of study / plans the course is directly associated with
- Analytical Biochemistry (programme PřF, N-BCH)
- Biochemistry (programme PřF, N-BCH)
- Genomics and Proteomics (programme PřF, D-BI4)
- Course objectives
- at the end of the course students should be able to: understand and explain terms related to proteomics; work with information on proteins and their complexes to follow their role in systems biology;
- Syllabus
- Jan Hejátko
- inroduction into proteomics – definition of proteome (dynamic p.), relations between genomics and proteomics, proteosynthesis and the basic hierarchy of protein structure, protein properties (size and shape, polarity, charge, reactivity))
- Jan Havliš
- expression proteomics - the conditions and regulation of gene products expression (under different conditions, also ontogenically) protein identity: protoprotein, protein splicing (intein, extein), post-translational modifications, transport, localisation of proteins (eg. cell membrane proteins, secretome), degradation, relations between genotype and phenotype
- Jaromír Marek
- structural proteomics - domains, tertiary structure, protein folding, structure and environment relations, allostery, structure modelling
- Jan Paleček
- functional proteomics - the role of proteins (enzymes, signalling molecules, transport molecules, structural molecules), relations between structure and function (domains, protein complexes), relations between localisation and function (interactive maps), relations between the content (and form) of protein and its function, interaction with aprotic molecules
- Zbyněk Zdráhal
- bioinformatics and proteins - Mw, pI, primary structure, PTMs, domains, tertiary structure, protein complexes, gene ontology (GO); phylogenetic similarity, the effect of mutations on the structure and function
- Zbyněk Zdráhal
- importance and use of proteomics - the contextual analytical proteomics, diagnostic proteomics (biomarkers), single cell proteomics, proteomic aspects of systems biology
- Literature
- Teaching methods
- the lecture is based on ppt presentations and their explication. presentations them-self will be available as study materials (black-and-white printable pdf with high resolution and restricted access rights). it is recommended to attend the lecture, because of the explication, which significantly extends the presentation and because there are no available textbooks in czech language covering certain parts of the subject.
- Assessment methods
- oral examination; students are required to understand and be familiar with the principles and its applications. examination consists of three basic questions, which would be during the examination expanded to let the student demonstrate the extent of topic understanding
- Language of instruction
- Czech
- Further Comments
- The course is taught annually.
The course is taught: every week. - Listed among pre-requisites of other courses
- Enrolment Statistics (recent)