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Cover Picture: Achieving Secondary Structural Resolution in Kinetic Measurements of Protein Folding: A Case Study of the Folding Mechanism of Trp-cage (Angew. Chem. Int. Ed. 46/2011)

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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Abstract

original image

The folding dynamics of individual structural elements in proteins is studied by a multi-probe and multi-frequency approach. In their Communication on page 10 884 ff., M. R. Bunagan, F. Gai, and co-workers achieve a significantly improved structural resolution in kinetic studies of protein folding using their approach. Application of this approach to the miniprotein Trp-cage provides new insights into the folding mechanism of this extensively studied protein.

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