What is the role of non-native intermediates of beta-lactoglobulin in protein folding?

Chikenji, G; Kikuchi, M · Proc Natl Acad Sci U S A · 2000

basic_science · Level V

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Abstract

The mechanism of alpha-->beta transition in folding of beta-lactoglobulin is discussed based on free energy landscape analysis of a long lattice model. It is found that helical propensity of beta-lactoglobulin is driven by conformational entropy and is intrinsically coded in its native structure. We propose a view on a role of folding intermediate, which is "on-pathway" but rich in non-native structures. The present results suggest that the native structure topology plays an important role in alpha-->beta transition.

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