Course Identification

Lecture 1 (27/10/20) DF
Course introduction
Protein primary structure: physical-chemical composition of proteins

Lecture 2 (3/11/20) DF
Protein secondary structure: helices, sheets, and beyond
Secondary structure propensities and prediction

Lecture 3 (10/11/20) RD
Tertiary structure: basic folding motifs, topology

Lecture 4 (17/11/20) DF
Quaternary structure: protein oligomerization

Lecture 5 (24/11/20) DF
Quaternary structure: polymerization and protein pathologies

Lecture 6 (1/12/20) RD
Principles, practices, challenges, and recent revolutions in protein structure determination I

Lecture 7 (8/12/20) RD
Principles, practices, challenges, and recent revolutions in protein structure determination II

Lecture 8 (15/12/20) DF
Protein thermodynamics

Lecture 9 (22/12/20) RD
Protein-protein interactions

Lecture 10 (29/12/20) DF
Protein folding, conformational changes, and dynamics in protein function I

Lecture 11 (5/1/21) DF
Protein folding, conformational changes, and dynamics in protein function II

Lecture 12 (12/1/21) RD
Enzymes

Lecture 13 (19/1/21) DF
Membrane proteins

Lecture 14 (26/1/21) RD
Molecular Machineries

Upon successful completion of this course students should be able to:

1. Describe fundamental hierarchy of protein structure, namely primary, secondary, tertiary, and quaternary structure.
2. Discuss how contemporary research still aims to refine our understanding of these basic concepts.
3. Describe principles of protein thermodynamics.
4. Demonstrate proficiency in various definitions of and approaches to the protein folding problem.
5. Discuss spectroscopic techniques in conjunction with the aspects of protein structure they probe, and particular challenges for the study of protein folding and stability in vivo.
6. Describe special classes of protein such as enzymes, chaperones, and membrane proteins.
7. Design and interpret experiments in structural biology and protein biochemistry.