Protein Physics

Part I INTRODUCTION Lecture 1: Main functions of proteins Part II ELEMENTARY INTERACTIONS IN AND AROUND PROTEINS Lecture 2: Amino acid residues in proteins Lecture 3: Quantum mechanics, Pauli exclusion principle, and non-covalent interactions Lecture 4: Influence of water environment Lecture 5: Water, hydrophobicity and proteins Lecture 6: Influence of an aqueous environment on electrostatic interactions Part III SECONDARY STRUCTURES OF POLYPEPTIDE CHAINS Lecture 7: Secondary structure of polypeptides Lecture 8: Elements of statistical mechanics Lecture 9: Free energy of initiation and elongation of a-helices in a homopolypeptide Lecture 10: 20 + 2 + 1 gene-coded amino acids in proteins Part IV PROTEIN STRUCTURES Lecture 11: Fibrous proteins, their functions, their regular primary and secondary structures Lecture 12: Membrane proteins; peculiarities of their structure and function Lecture 13: Globular proteins Lecture 14: Structure of a-proteins Lecture 15: Classification of protein folds Lecture 16: What secondary structure can be expected for random and quasi-random amino acid sequences Part V COOPERATIVE TRANSITIONS IN PROTEIN MOLECULES Lecture 17: "Well-folded" and "natively disordered" (or "intrinsically disordered") proteins Lecture 18: Denaturation of globular protein: why is it an "all-or-none" transition Lecture 19: Protein folding in vivo and in vitro Lecture 20: Two-state folding of small proteins: kinetic analog of the thermodynamic "all-or-none" transition Lecture 21: Solution of "Levinthal paradox" Part VI PREDICTION AND DESIGN OF PROTEIN STRUCTURE Lecture 22: Protein structure prediction from amino acid sequences Lecture 23: Overview of approaches to prediction and recognition of tertiary structures of proteins from their amino acid sequences Part VII PHYSICAL BACKGROUND OF PROTEIN FUNCTIONS Lecture 24: Protein function and protein structure Lecture 25: Combination of elementary functions Appendix A.: Theory of coil-globule transitions in