Conversion of two-state to multi-state folding kinetics on fusion of two protein foldons

Kenji Inaba, Naohiro Kobayashi, Alan R. Fersht

研究成果: Article査読

24 被引用数 (Scopus)

抄録

Chymotrypsin inhibitor 2 (CI2) is the archetypal single-foldon protein that folds in simple two-state kinetics without the accumulation of a folding intermediate. To model the effects of fusion of single foldons to give a multi-foldon protein, we engineered a 'double-CI2' protein, in which another CI2 polypeptide was inserted into the loop region of the parent CI2. CD and HSQC spectra demonstrated that while the double-CI2 protein adopted two kinds of native conformations, CI2-like structure was almost preserved in both the domains of double-CI2. In the folding kinetic studies, double-CI2 exhibited a remarkable rollover of the observed folding rates at low denaturant concentrations, indicating that double-CI2 accumulated a kinetic folding intermediate. The different folding mechanisms between WT-CI2 and double-CI2 support the present view that protein size or number of domains is an important determinant for formation of folding intermediates. (C) 2000 Academic Press.

本文言語English
ページ(範囲)219-233
ページ数15
ジャーナルJournal of Molecular Biology
302
1
DOI
出版ステータスPublished - 2000 9月 8
外部発表はい

ASJC Scopus subject areas

  • 構造生物学
  • 分子生物学

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