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.
journal_name
Proc Natl Acad Sci U S Aauthors
Akiyama S,Takahashi S,Kimura T,Ishimori K,Morishima I,Nishikawa Y,Fujisawa Tdoi
10.1073/pnas.012458999keywords:
subject
Has Abstractpub_date
2002-02-05 00:00:00pages
1329-34issue
3eissn
0027-8424issn
1091-6490pii
012458999journal_volume
99pub_type
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