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Achieving Secondary Structural Resolution in Kinetic Measurements of Protein Folding: A Case Study of the Folding Mechanism of Trp‐cage
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 - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201104085
Subject(s) - protein folding , folding (dsp implementation) , downhill folding , cage , chemical physics , twist , crystallography , temperature jump , mechanism (biology) , jump , helix (gastropod) , chemistry , biophysics , contact order , biological system , physics , phi value analysis , biology , mathematics , geometry , biochemistry , engineering , ecology , combinatorics , quantum mechanics , snail , electrical engineering
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 3 10 ‐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).