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Transient non-native helix formation during the folding of ?-lactoglobulin.

ABSTRACT: In ideal proteins, only native interactions are stabilized step-by-step in a smooth funnel-like energy landscape. In real proteins, however, the transient formation of non-native structures is frequently observed. In this review, the transient formation of non-native structures is described using the non-native helix formation during the folding of ?-lactoglobulin as a prominent example. Although ?-lactoglobulin is a predominantly ?-sheet protein, it has been shown to form non-native helices during the early stage of folding. The location of non-native helices, their stabilization mechanism, and their role in the folding reaction are discussed.

SUBMITTER: Ikeguchi M

PROVIDER: S-EPMC4030977 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature

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Transient non-native helix formation during the folding of β-lactoglobulin.

Ikeguchi Masamichi M

Biomolecules 20140213 1

In ideal proteins, only native interactions are stabilized step-by-step in a smooth funnel-like energy landscape. In real proteins, however, the transient formation of non-native structures is frequently observed. In this review, the transient formation of non-native structures is described using the non-native helix formation during the folding of β-lactoglobulin as a prominent example. Although β-lactoglobulin is a predominantly β-sheet protein, it has been shown to form non-native helices dur ...[more]

PMID: 24970212

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