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  • 标题:Ultrafast folding of WW domains without structured aromatic clusters in the denatured state
  • 本地全文:下载
  • 作者:Neil Ferguson ; Christopher M. Johnson ; Maria Macias
  • 期刊名称:Proceedings of the National Academy of Sciences
  • 印刷版ISSN:0027-8424
  • 电子版ISSN:1091-6490
  • 出版年度:2001
  • 卷号:98
  • 期号:23
  • 页码:13002-13007
  • DOI:10.1073/pnas.221467198
  • 语种:English
  • 出版社:The National Academy of Sciences of the United States of America
  • 摘要:Ultrafast-folding proteins are important for combining experiment and simulation to give complete descriptions of folding pathways. The WW domain family comprises small proteins with a three-stranded antiparallel {beta}-sheet topology. Previous studies on the 57-residue YAP 65 WW domain indicate the presence of residual structure in the chemically denatured state. Here we analyze three minimal core WW domains of 38-44 residues. There was little spectroscopic or thermodynamic evidence for residual structure in either their chemically or thermally denatured states. Folding and unfolding kinetics, studied by using rapid temperature-jump and continuous-flow techniques, show that each domain folds and unfolds very rapidly in a two-state transition through a highly compact transition state. Folding half-times were as short as 17 {micro}s at 25{degrees}C, within an order of magnitude of the predicted maximal rate of loop formation. The small size and topological simplicity of these domains, in conjunction with their very rapid two-state folding, may allow us to reduce the difference in time scale between experiment and theoretical simulation.
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