Course: Methods for Studying Structures and Interactions of Macromolecules

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Course title Methods for Studying Structures and Interactions of Macromolecules
Course code KBC/SSIM
Organizational form of instruction Lecture
Level of course Master
Year of study 2
Semester Summer
Number of ECTS credits 3
Language of instruction Czech
Status of course Compulsory-optional
Form of instruction Face-to-face
Work placements This is not an internship
Recommended optional programme components None
Lecturer(s)
  • Kopečný David, Mgr. Ph.D.
Course content
1. Optical rotational dispersion and circular dichroism, CD spectra of proteins and nucleic acids, static and dynamic light scattering, intereferometry on biological layer. 2. Small angle X-ray scattering (SAXS), Guinier graph, Kratky graph, paired distance distribution function, neutron scattering. 3. X-ray crystallography of biopolymers, crystal systems, Bravais lattices, Bragg's law, Miller indices, structural factors, measurement of X-ray diffraction, calculation of electron density map, phase problem, methods of anomalous scattering and isomorphic replacement, resolution. 4. Cryo-electron tomography (cryo-ET) and cryo-electron microscopy (cryo-EM), methods of positive and negative contrast. 5. Small-scale thermophoresis (MST), surface plasmon resonance (SPR). 7. Calorimetry, isothermal titration calorimetry (ITC), differential scanning calorimetry (DSC). 8. Fluorimetry, differential scanning fluorimetry (DSF), Förster resonance energy transfer (FRET), bimolecular fluorescence complementation (BiFC), membrane binding analysis (MeRA). 8. Voltammetric and polarographic analysis of macromolecules. 9. Yeast two-hybrid system (Y2H), equilibrium dialysis, co-immunoprecipitation, filter binding assay.

Learning activities and teaching methods
Lecture
  • Preparation for the Exam - 55 hours per semester
  • Attendace - 26 hours per semester
Learning outcomes
Students obtain information about methods focused on studying macromolecular structures (proteins and nucleic acids), their stability and further binding interactions such as protein / protein, protein / ligand, protein / nucleic acid.
Deeper insight into modern methods of biochemistry and structural biology obtained by attending the lecture KBC / SSIM focused on methods of studying macromolecule inerations supplemented with illustrative examples.
Prerequisites
The course is designed for master students of biochemistry and other students in chemical and biological fields.

Assessment methods and criteria
Oral exam

Passing the oral exam.
Recommended literature
  • Nordén, B., Rodger, A., Dafforn, T. (2010). Linear Dichroism and Circular Dichroism: A Textbook on Polarized-Light Spectroscopy. Cambridge.
  • Serdyuk, I. N., Nathan R., Zaccai, J. (2007). Methods in Molecular Biophysics : Structure, Dynamics, Function. Cambridge.
  • Waseda, Y., Matsubara, E., Shinoda, K. (2011). X-ray Diffraction Crystallography. Heidelberg.


Study plans that include the course
Faculty Study plan (Version) Category of Branch/Specialization Recommended year of study Recommended semester
Faculty: Faculty of Science Study plan (Version): Biochemistry (2022) Category: Chemistry courses 2 Recommended year of study:2, Recommended semester: Summer