Conformational Landscape of Cytochrome C Folding Studied by Microsecond-resolved Small-angle X-ray Scattering

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 2002 Jan 5

PMID 11773620

Citations 81

Authors

Shuji Akiyama

Satoshi Takahashi

Tetsunari Kimura

Koichiro Ishimori

Isao Morishima

Yukihiro Nishikawa

Tetsuro Fujisawa

Affiliations

Soon will be listed here.

Abstract

To investigate protein folding dynamics in terms of compactness, we developed a continuous-flow mixing device to make small-angle x-ray scattering measurements with the time resolution of 160 micros and characterized the radius of gyration (R(g)) of two folding intermediates of cytochrome c (cyt c). The early intermediate possesses approximately 20 A of R(g), which is smaller by approximately 4 A than that of the acid-unfolded state. The R(g) of the later intermediate is approximately 18 A, which is close to that of the molten globule state. Considering the alpha-helix content (f(H)) of the intermediates, we clarified the folding pathway of cyt c on the conformational landscape defined by R(g) and f(H). Cyt c folding proceeds with a collapse around a specific region of the protein followed by a cooperative acquisition of secondary structures and compactness.

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