Smaller and faster: the 20-residue Trp-cage protein folds in 4 micros

We have used laser temperature jump spectroscopy to measure the folding speed of the 20-residue Trp-cage, the smallest polypeptide known to exhibit truly cooperative folding behavior. The observed folding time (4 mus at room temperature) makes this not only the smallest foldable protein, but also th...

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Bibliographic Details
Published in:Journal of the American Chemical Society 2002-11, Vol.124 (44), p.12952-12953
Main Authors: Qiu, Linlin, Pabit, Suzette A, Roitberg, Adrian E, Hagen, Stephen J
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Circular Dichroism
Kinetics
Molecular Sequence Data
Oligopeptides - chemistry
Protein Folding
Spectrometry, Fluorescence
Tryptophan - chemistry
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Summary:We have used laser temperature jump spectroscopy to measure the folding speed of the 20-residue Trp-cage, the smallest polypeptide known to exhibit truly cooperative folding behavior. The observed folding time (4 mus at room temperature) makes this not only the smallest foldable protein, but also the fastest, with a folding speed that exceeds contact-order predictions and approaches anticipated diffusional "speed limits" for protein folding.
ISSN:0002-7863