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Structural Mapping of a Chaperone–Substrate Interaction Surface
Author(s) -
Callon Morgane,
Burmann Björn M.,
Hiller Sebastian
Publication year - 2014
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.201310963
Subject(s) - chaperone (clinical) , intermolecular force , chemistry , crystallography , biophysics , protein folding , nuclear magnetic resonance spectroscopy , stereochemistry , molecule , biochemistry , biology , medicine , pathology , organic chemistry
NMR spectroscopy is used to detect site‐specific intermolecular short‐range contacts in a membrane–protein–chaperone complex. This is achieved by an “orthogonal” isotope‐labeling scheme that permits the unambiguous detection of intermolecular NOEs between the well‐folded chaperone and the unfolded substrate ensemble. The residues involved in these contacts are part of the chaperone–substrate contact interface. The approach is demonstrated for the 70 kDa bacterial Skp‐tOmpA complex.