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Mapping Protein–Protein Interfaces on the Basis of Proton Density Difference
Author(s) -
Sui Xiaogang,
Xu Yingqi,
Giovannelli Janel L.,
Ho Nancy T.,
Ho Chien,
Yang Daiwen
Publication year - 2005
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.200501209
Subject(s) - protein subunit , protein structure , proton , docking (animal) , biological system , crystallography , chemistry , chemical physics , nuclear magnetic resonance , biophysics , materials science , physics , biology , biochemistry , medicine , nuclear physics , nursing , gene
Making contact : A protein–protein interface (see structure) can be identified unambiguously from the dependence of amide‐proton relaxation on proton density, as demonstrated by the identification of subunit contacts in hemoglobin. The information on upper limits for effective distances thus obtained allows the protein complex structure to be modeled more accurately with docking techniques.