Volume 50, Issue 46 p. 10735

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)

Robert M. Culik

Robert M. Culik

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

These authors contributed equally.

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Arnaldo L. Serrano

Arnaldo L. Serrano

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

These authors contributed equally.

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Prof. Dr. Michelle R. Bunagan

Corresponding Author

Prof. Dr. Michelle R. Bunagan

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

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

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

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Prof. Dr. Feng Gai

Corresponding Author

Prof. Dr. Feng Gai

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

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

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

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First published: 07 September 2011

Graphical Abstract

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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