C7920 Structure and functions of proteins

Faculty of Science
Autumn 2022
Extent and Intensity
2/0/0. 2 credit(s) (fasci plus compl plus > 4). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).
Teacher(s)
prof. RNDr. Břetislav Brzobohatý, CSc. (lecturer)
Mgr. Tomáš Klumpler, Ph.D. (lecturer)
doc. RNDr. Jaromír Marek, Ph.D. (lecturer)
Guaranteed by
prof. RNDr. Břetislav Brzobohatý, CSc.
National Centre for Biomolecular Research – Faculty of Science
Supplier department: National Centre for Biomolecular Research – Faculty of Science
Timetable
Wed 17:00–18:50 C03
Prerequisites
Completion of basic courses of biochemistry and/or molecular biology is a prerequisite for subscription to the course.
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
there are 9 fields of study the course is directly associated with, display
Course objectives
The course introduces students to the structure of proteins and to the dynamic behaviour of proteins & their combinations in relation to the biological functions of proteins.
Learning outcomes
The lecture summarises the basic knowledge about the structure and function of proteins. The first part of the lecture discusses the structural motifs of proteins, their stability and conformational dynamics. In the second part, selected biological functions of proteins (e.g., enzymes, membrane proteins, protein-ligand interactions) are discussed. In the third part, basic molecular biology techniques for protein isolation, gene cloning and expression, and structural biology for determining the 3D structures of proteins are presented.
Syllabus
  • 1. Basic structural principles of protein architecture. Building blocks of proteins. Protein structure motifs. Post-translational modifications of proteins. Stability and dynamics of proteins.
  • 2. Enzymes and enzyme catalysis. Proteins interacting with ligands (e.g., DNA and RNA molecules, transcription and translation factors). Membrane proteins, unstructured proteins.
  • 3. Methods of preparation of recombinant DNA molecules. Isolation and cloning of genes. DNA sequencing. Production of recombinant proteins. Prediction and modelling of protein structure. Biophysical methods for the determination of the 3D structure of proteins (protein crystallography, cryo-electron microscopy, NMR, SAXS).
Literature
    recommended literature
  • KESSEL, Amit a BEN-TAL Nir. Introduction to proteins. Structure, function and motion. 2nd ed. CRC Press, Taylor and Francis, Boca Raton, Florida USA, 2018, 880 s. ISBN 978-1-4987-4717-2
Teaching methods
lectures
Assessment methods
Oral exam or colloquium.
Language of instruction
Czech
Follow-Up Courses
Further Comments
Study Materials
The course can also be completed outside the examination period.
The course is taught annually.
Listed among pre-requisites of other courses
The course is also listed under the following terms Autumn 2007 - for the purpose of the accreditation, Autumn 1999, Autumn 2010 - only for the accreditation, Autumn 2000, Autumn 2001, Autumn 2002, Autumn 2003, Autumn 2004, Autumn 2005, Autumn 2006, Autumn 2007, Autumn 2008, Autumn 2009, Autumn 2010, Autumn 2011, Autumn 2011 - acreditation, Autumn 2012, Autumn 2013, Autumn 2014, Autumn 2015, Autumn 2016, autumn 2017, Autumn 2018, Autumn 2019, Autumn 2020, autumn 2021, Autumn 2023, Autumn 2024.
  • Enrolment Statistics (Autumn 2022, recent)
  • Permalink: https://is.muni.cz/course/sci/autumn2022/C7920