Thermodynamics and kinetics of protein folding under confinement.

ABSTRACT: Understanding the effects of confinement on protein stability and folding kinetics is important for describing protein folding in the cellular environment. We have investigated the effects of confinement on two structurally distinct proteins as a function of the dimension d(c) and characteristic size R of the confining boundary. We find that the stabilization of the folded state relative to bulk conditions is quantitatively described by R(-gamma(c)), where the exponent gamma(c) is approximately 5/3 independent of the dimension of confinement d(c) (cylindrical, planar, or spherical). Moreover, we find that the logarithm of the folding rates also scale as R(-gamma(c)), with deviations only being seen for very small confining geometries, where folding is downhill; for both stability and kinet

SUBMITTER: Mittal J 

PROVIDER: S-EPMC2629327 | biostudies-literature | 2008 Dec

REPOSITORIES: biostudies-literature