Structural Mapping of a Chaperone- Substrate Interaction Surface**
Structural Mapping of a Chaperone- Substrate Interaction Surface**
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DOI:
10.1002/anie.201310963
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发表时间:
2014-05-12
影响因子:
16.6
通讯作者:
Hiller, Sebastian
中科院分区:
文献类型:
--
作者:
Callon, Morgane;Burmann, Bjoern M.;Hiller, Sebastian
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 70kDa bacterial Skp-tOmpA complex.