In:
Proceedings of the National Academy of Sciences, Proceedings of the National Academy of Sciences, Vol. 99, No. 3 ( 2002-02-05), p. 1329-1334
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 μs and characterized the radius of gyration ( R g ) of two folding intermediates of cytochrome c (cyt c ). The early intermediate possesses ≈20 Å of R g , which is smaller by ≈4 Å than that of the acid-unfolded state. The R g of the later intermediate is ≈18 Å, which is close to that of the molten globule state. Considering the α-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.
Type of Medium:
Online Resource
ISSN:
0027-8424
,
1091-6490
DOI:
10.1073/pnas.012458999
Language:
English
Publisher:
Proceedings of the National Academy of Sciences
Publication Date:
2002
detail.hit.zdb_id:
209104-5
detail.hit.zdb_id:
1461794-8
SSG:
11
SSG:
12
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