These authors contributed equally.
Achieving Secondary Structural Resolution in Kinetic Measurements of Protein Folding: A Case Study of the Folding Mechanism of Trp-cage†
Article first published online: 29 SEP 2011
Copyright © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Angewandte Chemie International Edition
Volume 50, Issue 46, pages 10884–10887, November 11, 2011
How to Cite
Culik, R. M., Serrano, A. L., Bunagan, M. R. and Gai, F. (2011), Achieving Secondary Structural Resolution in Kinetic Measurements of Protein Folding: A Case Study of the Folding Mechanism of Trp-cage. Angew. Chem. Int. Ed., 50: 10884–10887. doi: 10.1002/anie.201104085
We thank the National Institutes of Health (GM-065978, RR01348, and GM-008275) for funding. R.M.C. acknowledges a training grant in structural biology.
- Issue published online: 9 NOV 2011
- Article first published online: 29 SEP 2011
- Manuscript Received: 14 JUN 2011
- National Institutes of Health. Grant Numbers: GM-065978, RR01348, GM-008275
- IR spectroscopy;
- protein folding;
A new twist: A multi-probe and multi-frequency approach is shown for dissecting the folding dynamics of individual protein structural elements. In response to a temperature jump the 310-helix (blue in the picture) of the miniprotein Trp-cage unfolds before the global unfolding of the protein, whereas the formation of the cage structure depends on the folding of the α-helix (red).