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

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

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
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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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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