HHMI%20meeting,%20FOLDING

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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.

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Solid structures
However, solid structures can denaturate (decay)
both in vivo (e.g., when protein is transported
through membrane) and in vitro
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Protein denaturation cooperative transition
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Denaturation all-or-none transition in
small (one-domain) proteins
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Denaturation all-or-none transition
in small (one-domain) proteins
(Privalov, 1969)
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Solid native state, unfolded coil, more compact
molten state and cooperative transitions between
them
?
(Tanford, 1968)
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Secondary structure Side chain packing
un- folded
native
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All-or-none decay of native protein
structure Ensures reliability and robustness
of protein functioning