期刊
JOURNAL OF MOLECULAR BIOLOGY
卷 368, 期 1, 页码 219-229出版社
ACADEMIC PRESS LTD ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2007.01.085
关键词
protein folding; folding intermediate; small-angle X-ray scattering; hydrophobic collapse; native structure
资金
- NCRR NIH HHS [RR-08630] Funding Source: Medline
Using small-angle X-ray scattering combined with a continuous-flow mixing device, we monitored the microsecond compaction dynamics in the folding of Escherichia coli dihydrofolate reductase, an alpha/beta-type protein. A significant collapse of the radius of gyration from 30 angstrom to 23.2 angstrom occurs within 300 mu s after the initiation of refolding by a urea dilution jump. The subsequent folding after the major chain collapse occurs on a considerably longer timescale. The protein folding trajectories constructed by comparing the development of the compactness and the secondary structure suggest that the specific hydrophobic collapse model rather than the framework model better explains the experimental observations. The folding trajectory of this alpha/beta-type protein is located between those of alpha-helical and beta-sheet proteins, suggesting that native structure determines the folding landscape.
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