Communication

Achieving Secondary Structural Resolution in Kinetic Measurements of Protein Folding: A Case Study of the Folding Mechanism of Trp-cage†

  1. Robert M. Culik3,‡,
  2. Arnaldo L. Serrano1,‡,
  3. Prof. Dr. Michelle R. Bunagan2,*,
  4. Prof. Dr. Feng Gai1,*

Article first published online: 29 SEP 2011

DOI: 10.1002/anie.201104085

Issue

Angewandte Chemie International Edition

Angewandte Chemie International Edition

Volume 50, Issue 46, pages 10884–10887, November 11, 2011

Additional Information

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

Author Information

  1. 1

    Department of Chemistry, University of Pennsylvania, 231 S. 34 Street, Philadelphia, PA 19104 (USA)

  2. 2

    Department of Chemistry, College of New Jersey, 2000 Pennington Road, Ewing, NJ 08628 (USA)

  3. 3

    Department of Biochemistry and Molecular Biophysics, University of Pennsylvania (USA)

  1. ‡

    These authors contributed equally.

*Department of Chemistry, College of New Jersey, 2000 Pennington Road, Ewing, NJ 08628 (USA)

  1. †

    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.

  2. ‡

    These authors contributed equally.

Publication History

  1. Issue published online: 9 NOV 2011
  2. Article first published online: 29 SEP 2011
  3. Manuscript Received: 14 JUN 2011

Funded by

  • National Institutes of Health. Grant Numbers: GM-065978, RR01348, GM-008275

SEARCH

SEARCH BY CITATION

ARTICLE TOOLS

View Full Article with Supporting Information (HTML) Get PDF (601K)

Keywords:

  • IR spectroscopy;
  • kinetics;
  • protein folding;
  • proteins
Thumbnail image of graphical abstract

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).

View Full Article with Supporting Information (HTML) Get PDF (601K)