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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)
Author(s) -
Culik Robert M.,
Serrano Arnaldo L.,
Bunagan Michelle R.,
Gai Feng
Publication year - 2011
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201106049
Subject(s) - folding (dsp implementation) , protein folding , cover (algebra) , chemistry , cage , mechanism (biology) , kinetic energy , downhill folding , crystallography , chemical physics , biophysics , phi value analysis , physics , biochemistry , biology , engineering , mechanical engineering , structural engineering , quantum mechanics , electrical engineering
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.