TY - JOUR
T1 - Conformational landscape of cytochrome c folding studied by microsecond-resolved small-angle x-ray scattering
AU - Akiyama, Shuji
AU - Takahashi, Satoshi
AU - Kimura, Tetsunari
AU - Ishimori, Koichiro
AU - Morishima, Isao
AU - Nishikawa, Yukihiro
AU - Fujisawa, Tetsuro
PY - 2002/2/5
Y1 - 2002/2/5
N2 - To investigate protein folding dynamics in terms of compactness, we developed a continuous-flow mixing device to make smallangle x-ray scattering measurements with the time resolution of 160 μs and characterized the radius of gyration (Rg) of two folding intermediates of cytochrome c (cyt c). The early intermediate possesses ≈-20 Å of Rg, which is smaller by ≈-4 A than that of the acid-unfolded state. The Rg of the later intermediate is ≈-18 Å, which is close to that of the molten globule state. Considering the α-helix content (fH) of the intermediates, we clarified the folding pathway of cyt c on the conformational landscape defined by Rg and fH- Cyt c folding proceeds with a collapse around a specific region of the protein followed by a cooperative acquisition of secondary structures and compactness.
AB - To investigate protein folding dynamics in terms of compactness, we developed a continuous-flow mixing device to make smallangle x-ray scattering measurements with the time resolution of 160 μs and characterized the radius of gyration (Rg) of two folding intermediates of cytochrome c (cyt c). The early intermediate possesses ≈-20 Å of Rg, which is smaller by ≈-4 A than that of the acid-unfolded state. The Rg of the later intermediate is ≈-18 Å, which is close to that of the molten globule state. Considering the α-helix content (fH) of the intermediates, we clarified the folding pathway of cyt c on the conformational landscape defined by Rg and fH- 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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U2 - 10.1073/pnas.012458999
DO - 10.1073/pnas.012458999
M3 - Article
C2 - 11773620
AN - SCOPUS:0037022327
SN - 0027-8424
VL - 99
SP - 1329
EP - 1334
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
IS - 3
ER -