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

Authors

  • Robert M. Culik,

    1. Department of Biochemistry and Molecular Biophysics, University of Pennsylvania (USA)
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    • These authors contributed equally.

  • Arnaldo L. Serrano,

    1. Department of Chemistry, University of Pennsylvania, 231 S. 34 Street, Philadelphia, PA 19104 (USA)
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    • These authors contributed equally.

  • Prof. Dr. Michelle R. Bunagan,

    Corresponding author
    1. Department of Chemistry, College of New Jersey, 2000 Pennington Road, Ewing, NJ 08628 (USA)
    • Department of Chemistry, College of New Jersey, 2000 Pennington Road, Ewing, NJ 08628 (USA)
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  • Prof. Dr. Feng Gai

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

Abstract

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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).

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