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Kim, Taewu
나노물질 및 화학반응 연구단
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Protein folding from heterogeneous unfolded state revealed by time-resolved X-ray solution scattering

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Title
Protein folding from heterogeneous unfolded state revealed by time-resolved X-ray solution scattering
Author(s)
Tae Wu Kim; Sang Jin Lee; Junbeom Jo; Jong Goo Kim; Hosung Ki; Chang Woo Kim; Kwang Hyun Cho; Jungkweon Choi; Jae Hyuk Lee; Michael Wulff; Young Min Rhee; Hyotcherl Ihee
Subject
cytochrome c, ; ensemble, ; molecular dynamics simulation, ; protein folding, ; time-resolved X-ray scattering
Publication Date
2020-06
Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, v.117, no.26, pp.14996 - 15005
Publisher
NATL ACAD SCIENCES
Abstract
© 2020 National Academy of Sciences. One of the most challenging tasks in biological science is to understand how a protein folds. In theoretical studies, the hypothesis adopting a funnel-like free-energy landscape has been recognized as a prominent scheme for explaining protein folding in views of both internal energy and conformational heterogeneity of a protein. Despite numerous experimental efforts, however, comprehensively studying protein folding with respect to its global conformational changes in conjunction with the heterogeneity has been elusive. Here we investigate the redox-coupled folding dynamics of equine heart cytochrome c (cyt-c) induced by external electron injection by using time-resolved X-ray solution scattering. A systematic kinetic analysis unveils a kinetic model for its folding with a stretched exponential behavior during the transition toward the folded state. With the aid of the ensemble optimization method combined with molecular dynamics simulations, we found that during the folding the heterogeneously populated ensemble of the unfolded state is converted to a narrowly populated ensemble of folded conformations. These observations obtained from the kinetic and the structural analyses of X-ray scattering data reveal that the folding dynamics of cyt-c accompanies many parallel pathways associated with the heterogeneously populated ensemble of unfolded conformations, resulting in the stretched exponential kinetics at room temperature. This finding provides direct evidence with a view to microscopic protein conformations that the cyt-c folding initiates from a highly heterogeneous unfolded state, passes through still diverse intermediate structures, and reaches structural homogeneity by arriving at the folded state
URI
https://pr.ibs.re.kr/handle/8788114/7803
DOI
10.1073/pnas.1913442117
ISSN
0027-8424
Appears in Collections:
Center for Nanomaterials and Chemical Reactions(나노물질 및 화학반응 연구단) > 1. Journal Papers (저널논문)
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