Smaller and Faster:  The 20-Residue Trp-Cage Protein Folds in 4 μs

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 μs at room temperature) makes this not only the smallest foldable protein, but also the...

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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:
Atomic and molecular physics
Biological and medical sciences
Calculations and mathematical techniques in atomic and molecular physics (excluding electron correlation calculations)
Computational techniques
Conformational dynamics in molecular biology
Electronic structure of atoms, molecules and their ions: theory
Exact sciences and technology
Fundamental and applied biological sciences. Psychology
Mathematical methods in physics
Molecular biophysics
Molecular dynamics and other numerical methods
Molecular dynamics and particle methods
Physics
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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 μs 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
1520-5126
DOI:10.1021/ja0279141