TITLE

Folding at the speed limit

AUTHOR(S)
Yang, Wei Yuan; Gruebele, Martin
PUB. DATE
May 2003
SOURCE
Nature;5/8/2003, Vol. 423 Issue 6936, p193
SOURCE TYPE
Academic Journal
DOC. TYPE
Article
ABSTRACT
Many small proteins seem to fold by a simple process explicable by conventional chemical kinetics and transition-state theory. This assumes an instant equilibrium between reactants and a high-energy activated state[SUP1]. In reality, equilibration occurs on timescales dependent on the molecules involved, below which such analyses break down[SUP1]. The molecular timescale, normally too short to be seen in experiments, can be of a significant length for proteins. To probe it directly, we studied very rapidly folding mutants of the five-helix bundle protein λ[SUB6-85], whose activated state is significantly populated during folding. A time-dependent rate coefficient below 2μs signals the onset of the molecular timescale, and hence the ultimate speed limit for folding[SUP2]. A simple model shows that the molecular timescale represents the natural pre-factor for transition state models of folding.
ACCESSION #
9700592

 

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