Journal
BIOMOLECULES
Volume 4, Issue 1, Pages 202-216Publisher
MDPI AG
DOI: 10.3390/biom4010202
Keywords
alpha-helix; beta-sheet; stopped-flow; circular dichroism; hydrogen-deuterium exchange; mutant protein
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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 beta-lactoglobulin as a prominent example. Although beta-lactoglobulin is a predominantly beta-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.
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