Protein Structures: Thermodynamic Aspects (1)

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Presentation transcript:

Protein Structures: Thermodynamic Aspects (1) PROTEIN PHYSICS LECTURE 17 Protein Structures: Thermodynamic Aspects (1) Protein denaturation: reversible, cooperative and, moreover, “all-or-none” (1-st order) phase transition. Solid native state, unfolded coil & “molten globule”.

Solid structures However, solid structures can denaturate (decay) both in vivo (e.g., when protein is transported through membrane) and in vitro

Protein denaturation: cooperative transition

Denaturation: “all-or-none” transition in small (one-domain) proteins

Denaturation: “all-or-none” transition in small (one-domain) proteins (Privalov, 1969)

Solid native state, unfolded coil, “more compact molten state” and cooperative transitions between them ? (Tanford, 1968)

Secondary structure Side chain packing unfolded native

“All-or-none” decay of native protein structure: Ensures reliability and robustness of protein functioning