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Relationship between chain collapse and secondary structure formation in a partially folded protein
Author(s) -
Nakagawa Kanako,
Yamada Yoshiteru,
Matsumura Yoshitaka,
Tsukamoto Seiichi,
YamamotoOhtomo Mio,
Ohtomo Hideaki,
Okabe Takahiro,
Fujiwara Kazuo,
Ikeguchi Masamichi
Publication year - 2014
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.22433
Subject(s) - chemistry , radius of gyration , protein secondary structure , folding funnel , folding (dsp implementation) , molten globule , protein folding , gyration , crystallography , chemical physics , chain (unit) , small angle x ray scattering , polymer , phi value analysis , scattering , downhill folding , biochemistry , organic chemistry , physics , geometry , mathematics , optics , astronomy , electrical engineering , engineering
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.