Содержание
- 2. Natively disordered proteins in vivo - no 3D structure under physiological conditions • Disordered states can
- 3. Acceleration of molecular recognition One protein – several functions Protein’s conformation is determined by the interaction
- 4. Protein denaturation in vitro: cooperative transition Solid protein structures can denaturate (decay), and then re-nature (fold)
- 5. transition
- 6. Denaturation: “all-or-none” transition in small (single-domain) proteins (Privalov, 1969) For a melting unit: T0ΔS1=ΔE1 Transition: |ΔG1|=
- 7. ΔS/k >> 1 T0=ΔE/ΔS
- 8. Jacobus Henricus van 't Hoff, Jr. (1852 –1911) The first Nobel prize in Chemistry, 1901 ПРИВАЛОВ
- 10. “All-or-none” decay of native protein structure: Ensures reliability and robustness of protein functioning Solid native state,
- 11. IN VARIOUS STATES: Secondary structure Side chain packing native un- folded native
- 12. “all-or-none” “all-or -none” “all-or-one”? sharp but gradual?
- 13. Евгений Исаакович Шахнович, 1957 Дмитрий Александрович Долгих, 1954 Геннадий Васильевич Семисотнов, 1947 Олег Борисович Птицын (1929-99)
- 14. Why protein denaturation is an “all-or-none” phase transition? Peculiarities of protein structure: - Unique fold; -
- 15. Start of the side chain liberation “All-or-none” melting:
- 16. “All-or-none” melting: a result of the “ENERGY GAP” Start of the side chain liberation ~ ln[M(E)]
- 17. “all-or-none” transition results from the “energy gap” Energy landscape The “energy gap” is: - necessary for
- 18. GAP WIDTH: MAIN PROBLEM OF EXPERIMENTAL PROTEIN PHYSICS PHYSICAL ESTIMATE: =??? BIOLOGICAL ESTIMATE: 1 0F ~1010
- 19. e PROTEIN FOLDING: current picture (Dobson, 2003) (MG)
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