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Interactions with Hydrophobic Clusters in the Urea‐Unfolded Membrane Protein OmpX
Author(s) -
Hiller Sebastian,
Wider Gerhard,
Imbach Lukas L.,
Wüthrich Kurt
Publication year - 2008
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.200703367
Subject(s) - folding (dsp implementation) , urea , micelle , chemistry , protein folding , amino acid , hydrophobic effect , crystallography , biophysics , biochemistry , biology , organic chemistry , engineering , aqueous solution , electrical engineering
A denatured membrane protein in 8 M urea was characterized. Two hydrophobic clusters, separated by 50 amino acids in the polypeptide chain, are shown to bind independently to detergent micelles (see picture). Long‐range interactions between the two clusters are not observed. These observations provide new insights into protein folding mechanisms.