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Biomolecules 2014, 4(1), 202-216; doi:10.3390/biom4010202

Transient Non-Native Helix Formation during the Folding of β-Lactoglobulin

Department of Bioinformatics, Soka University, 1-236 Tangi-cho, Hachioji, Tokyo 192-8577, Japan
Received: 6 January 2014 / Revised: 5 February 2014 / Accepted: 10 February 2014 / Published: 13 February 2014
(This article belongs to the Special Issue Protein Folding and Misfolding)
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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 β-lactoglobulin as a prominent example. Although β-lactoglobulin is a predominantly β-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.
Keywords: α-helix; β-sheet; stopped-flow; circular dichroism; hydrogen-deuterium exchange; mutant protein α-helix; β-sheet; stopped-flow; circular dichroism; hydrogen-deuterium exchange; mutant protein
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This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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Ikeguchi, M. Transient Non-Native Helix Formation during the Folding of β-Lactoglobulin. Biomolecules 2014, 4, 202-216.

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