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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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Eine überraschende Wendung: Eine neuartige Multisonden- und Multifrequenzmethode ermöglicht die Untersuchung der Faltungsdynamik individueller Proteinstrukturelemente. Ausgelöst durch einen Temperatursprung entfaltet sich die 310-Helix (blau im Bild) des Miniproteins Trp-cage vor der globalen Entfaltung des Proteins, während die Bildung der Käfigstruktur von der Faltung der α-Helix (rot) abhängt.

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