Inhalt

[ 863ABBCPRC12 ] Module Protein Chemistry

Versionsauswahl
Es ist eine neuere Version 2018W dieses Fachs/Moduls im Curriculum Master's programme Joint Master Programme Biological Chemistry 2018W vorhanden.
Workload Mode of examination Education level Study areas Responsible person Coordinating university
4 ECTS Accumulative module examination M2 - Master's programme 2. year (*)Biologische Chemie Rüdiger Ettrich / Libor Grubhoffer USB Budweis
Detailed information
Original study plan Master's programme Joint Master Programme Biological Chemistry 2015W
Objectives The course focuses on the chemistry of peptides and proteins as well as physical and chemical methods applied to the studies of protein structure, protein structures in relation to their function, and the structure of proteins.

Students will acquire practical hands-on experience in the field of protein chemistry.

Subject The course reviews the chemistry of peptides and proteins: Polymer of amino acid, the backbone of a polymer; Three-dimensional structure: Secondary structure, Fibrous proteins, Globular proteins, Protein stability, Quaternary structure; Protein folding and dynamics: Protein folding, theory and experiment, protein denaturation, folding pathway and prediction of protein structure; Protein dynamics; atomic fluctuations, collective motions and triggered, conformational changes; Experimental methods applied to study protein structures: Transport in electric field, Scattering by larger particles (X-rays diffraction by fibrous proteins, NMR, Circular dichroism, Laser raman, Neutron diffraction; Theoretical methods applied to study protein structures: homolgy modeling, molecular dynamics, ligand/docking, coarse graining; Allosteric regulation; Adair equation, Symmetry model, Sequential model and cooperativity.

Exercising and discussing recently learned material from the course in protein chemistry.

Further information Learning Goals. Students will:

• acquire detailed insight into the structure of proteins with respect to protein chemical and biophysical experiments

• acquire insight into the use of prediction methods and molecular modeling techniques

• acquire knowledge and insight into protein folding in vitro and comparison to in vivo protein folding

• acquire knowledge and insight into the general principles of protein purification (based on size, charge, hydrophobicity or on biospecific properties)

• acquire knowledge of possible chemical modification reactions

Corresponding lecture VL Protein Chemistry (3 ECTS) + SE Protein Chemistry Seminar (1 ECTS) (as lecture)
Subordinated subjects, modules and lectures