Relationship between chain collapse and secondary structure formation in a partially folded protein. Issue 6 (June 2014)

• Record Type: Journal Article
• Authors: Nakagawa, Kanako; Yamada, Yoshiteru; Matsumura, Yoshitaka; Tsukamoto, Seiichi; Yamamoto‐Ohtomo, Mio; Ohtomo, Hideaki; Okabe, Takahiro; Fujiwara, Kazuo; Ikeguchi, Masamichi
• Is Part Of: Biopolymers. Volume 101:Issue 6(2014)
• Page Start: 651
• Page End: 658
• Publication Date: 2014-06
• Subjects: Biopolymers -- Periodicals; Peptides -- Periodicals; Spectrum analysis -- Periodicals; 572.33
• DOI: 10.1002/bip.22433
• Languages: English
• ISSNs: 0006-3525

Abstract

<abstract abstract-type="main"> <title>ABSTRACT</title> <p>Chain collapse and secondary structure formation are frequently observed during the early stages of protein folding. Is the chain collapse brought about by interactions between secondary structure units or is it due to polymer behavior in a poor solvent (coil‐globule transition)? To answer this question, we measured small‐angle X‐ray scattering for a series of β‐lactoglobulin mutants under conditions in which they assume a partially folded state analogous to the folding intermediates. Mutants that were designed to disrupt the secondary structure units showed the gyration radii similar to that of the wild type protein, indicating that chain collapse is due to coil‐globule transitions. © 2013 Wiley Periodicals, Inc. Biopolymers 101: 651–658, 2014.</p> </abstract>