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Direct Prediction of NMR Residual Dipolar Couplings from the Primary Sequence of Unfolded Proteins
Author(s) -
Huang Jierong,
Ozenne Valéry,
Jensen Malene Ringkjøbing,
Blackledge Martin
Publication year - 2013
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.201206585
Subject(s) - residual , dipole , residual dipolar coupling , computer science , chemistry , sequence (biology) , computational biology , algorithm , biology , biochemistry , organic chemistry
Conformational analysis : An approach to the prediction of RDCs from disordered protein chains, integrating the effect of nearest neighbors and the alignment characteristics of the statistical coil, is reported. NMR residual dipolar couplings (RDC) are sensitive probes of conformational sampling in unfolded proteins (see picture).