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Evidence for a Broad Transition‐State Ensemble in Calmodulin Folding from Single‐Molecule Force Spectroscopy
Author(s) -
Junker Jan Philipp,
Rief Matthias
Publication year - 2010
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.200905747
Subject(s) - calmodulin , force spectroscopy , folding (dsp implementation) , protein folding , spectroscopy , molecule , energy landscape , chemical physics , chemistry , downhill folding , biophysics , transition (genetics) , crystallography , phi value analysis , physics , biology , calcium , biochemistry , engineering , quantum mechanics , organic chemistry , electrical engineering , gene
Same difference : Single‐molecule force spectroscopy was used to study folding and unfolding pathways of calmodulin. Depending on the force application points, different pathways that are similar in energy can be populated. Such a broad transition‐state ensemble has been postulated for ultrafast protein folding.