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- W2113227718 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." @default.
- W2113227718 created "2016-06-24" @default.
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- W2113227718 date "2002-01-02" @default.
- W2113227718 modified "2023-10-11" @default.
- W2113227718 title "Conformational landscape of cytochrome <i>c</i> folding studied by microsecond-resolved small-angle x-ray scattering" @default.
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- W2113227718 doi "https://doi.org/10.1073/pnas.012458999" @default.
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