C6200 Biochemical Methods

Faculty of Science
Spring 2007
Extent and Intensity
4/0/0. 4 credit(s) (fasci plus compl plus > 4). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).
Teacher(s)
prof. RNDr. Zdeněk Glatz, CSc. (lecturer)
prof. RNDr. Vladimír Mikeš, CSc. (lecturer)
doc. RNDr. Petr Zbořil, CSc. (lecturer)
Guaranteed by
prof. RNDr. Vladimír Mikeš, CSc.
Department of Biochemistry – Chemistry Section – Faculty of Science
Timetable
Tue 9:00–10:50 C02/121, Tue 13:00–14:50 C02/121
Prerequisites
Basic knowledge of biochemistry, 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
Course objectives
Basic methods of desintegration of animal, vegetal and microbial tissues. Methods of isolation, purification of enzymes and biopolymers. Determination of purity and molecular properties of enzymes. Spectroscopic, electrochemical and physical methods of analysis in biochemistry.
Syllabus
  • 1. Introduction, the strategy of treatement of biological material 2. Desintegration, centrifugation, sedimentation analysis 3. Phase separation, precipitation, extraction. membrane separation, Concentration and lyophilisation, water treatment 4. Chromatoigrafic methods, principles (adsorption, ion-exchange), chromatofocusation 5. Reversed phase chromatography, ion pair chromatography, hydrophobic, GPC, affinity, gaz chromatography 6. Electromigration methods, principles, zone electrophoresis 7. IEF, isotachophoresis, blotting 8. Methods of determination of mol. mass and shape of molecules, mass spectrometry, Osmometry, Viscosimetry, translation and rotation diffusion 9. X-ray analysis, electrochemical methods, principles, potentiometry, ISE, biosensors 10. Amperometry, polaropgraphy, voltametry, calorimetry, biochemical applications. Fast reactions, ion exchange, ligand-polymer interactions, methods of determoination binding parameters. 11. Spectroketry. Electron spectra, transitions, groun and excited state, influence of solvents, UV-VIS spectrometry. Use for the study of protein structure 12. Luminiscence methods. Physical parameters, fluorescence quenching, energy transfer, fluorescence polarisation,phosphorimetry, 13. IR spctroscopy, Raman spectroscopy, ORD, CD 14. NMR, EPR, Mossbauer spectroscopy
Literature
  • KALOUS, Vítěz. Metody chemického výzkumu. 1. vyd. Praha: SNTL - Nakladatelství technické literatury, 1987, 430 s. URL info
  • ANZENBACHER, Pavel and Jan KOVÁŘ. Metody chemického výzkumu pro biochemiky. 1. vyd. Praha: Ministerstvo školství ČSR, 1986, 199 s. info
  • KALOUS, Vítěz and Zdeněk PAVLÍČEK. Biofyzikální chemie. 1. vyd. Praha: Nakladatelství technické literatury, 1980, 349 s. info
Assessment methods (in Czech)
Základní přednáška, na které se podílí více vyučujících, včetně externistů
Language of instruction
Czech
Follow-Up Courses
Further comments (probably available only in Czech)
Study Materials
The course is taught each semester.
General note: Vyučují učitelé katedry biochemie.
Listed among pre-requisites of other courses
The course is also listed under the following terms Spring 2008 - for the purpose of the accreditation, Spring 2011 - only for the accreditation, Spring 2000, Spring 2001, Spring 2002, Spring 2003, Spring 2004, Spring 2005, Spring 2006, Spring 2008, Spring 2009, Spring 2010, Spring 2011, Spring 2012, spring 2012 - acreditation, Spring 2013, Spring 2014, Spring 2015, Spring 2016, Spring 2017, spring 2018, Spring 2019, Spring 2020, Spring 2021, Spring 2022, Spring 2023, Spring 2024, Spring 2025.
  • Enrolment Statistics (Spring 2007, recent)
  • Permalink: https://is.muni.cz/course/sci/spring2007/C6200