Содержание
- 2. Олег Борисович Птицын (1929-1999)
- 3. PROTEIN PHYSICS LECTURE 1 Introduction & overview
- 4. Globular proteins Fibrous proteins H-bonds (NH:::OC) & hydrophobic forces Membrane proteins
- 5. Protein chain (gene-encoded sequence)
- 6. Secondary structures (α-helices, β-strands) are most conserved structural elements. They form a basis of protein classification
- 9. Globular proteins Fibrous proteins H-bonds (NH:::OC) & hydrophobic forces Membrane proteins Sequence & Structure
- 10. Globular domains C A T H
- 11. PROTEIN CHAIN CAN FORM ITS UNIQUE 3D STRUCTURE SPONTANEOUSLY IN VITRO
- 12. phase separation
- 13. BIND ? TRANSFORM ? RELEASE: ENZYMES (chymotrypsin) Note small active site
- 14. POST-TRANSLATIONAL MODIFICATIONS Sometimes, CHAIN CUT-INDUCED DEFORMATION MAKES ENZYME ACTIVE Chymotripsin Chymotripsinogen active cat. site non-active cat.
- 15. POST-TRANSLATIONAL MODIFICATIONS: (especially in eukaryotes): PROTEIN CHAIN CUTS (proteolysis), - SPLICING (inteins) - CYCLIZATION - INTERNAL
- 16. Sometimes: Different folds with the same active site: the same biochemical function
- 17. Sometimes: Similar folds with different active sites: different biochemical function 4-helix bundle COFACTORS: HEME, 2Fe, RNA,
- 18. Standard positions of active sites in protein folds
- 19. Natively disordered protein: X-ray + SAXS + NMR + MD simulations
- 20. Chaperone GroEL
- 21. ______ NMR
- 22. Protein engineering Wanted: new protein with additional salt bridge (e.g., His+:::Asp-)
- 23. PROTEIN PHYSICS LECTURE 2 Elementary interactions: covalent
- 24. Protein chain: regular backbone & gene-encoded sequence of side chains
- 25. Protein chain Covalent bond lengths: 0.9 – 1.8 Å Covalent bond angles: 109o – 120o Atom
- 26. Side chains
- 27. Main-chain: peptide group: flat & rigid Side chains: L amino acids ___ ______ ______ Protein chain
- 28. Ala _L Gly Thr Ile Two asymmetric side chains: Symmetric Asymmetric backbone-to- side_chain: Stereo images
- 29. ~ V = ±|V| ≅ semi-classical approximation
- 30. Werner Karl Heisenberg (1901-76) — Nobel Prize 1932 Wolfgang Ernst Pauli ) (1900-58) — Nobel Prize
- 31. Peptide group: flat & rigid sp2 + p sp2 + p Covalent bonding in peptide group:
- 32. Main-chain: φ (N-Cα) , ψ (Cα-C’), ω (C’=N) Side-chain: χ1, χ2, ...
- 33. Counting angles: _____________________________________________ 0o 180o 120o
- 34. sp2 - sp2 (ω) ω = 180o ω = 0o
- 35. Potentials: from IR spectra of vibrations sp2 - sp2 (ω) sp3 – sp3 (χ) sp2 –
- 36. Harold Abraham Scheraga (1921) Paul John Flory (1910-85) — Nobel Prize 1974 Александр Исаакович Китайгородский (1914–1985)
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