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Protein Conformational Space Populated in Solution Probed with Aromatic Residual Dipolar 13 C– 1 H Couplings
Author(s) -
Sathyamoorthy Bharathwaj,
Singarapu Kiran K.,
Garcia Angel E.,
Szyperski Thomas
Publication year - 2013
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201300016
Subject(s) - excited state , chemistry , residual dipolar coupling , characterization (materials science) , dipole , linear subspace , protein structure , molecule , nuclear magnetic resonance spectroscopy , chemical physics , computational chemistry , crystallography , stereochemistry , physics , nanotechnology , atomic physics , materials science , organic chemistry , biochemistry , geometry , mathematics
The use of aromatic 13 C– 1 H residual dipolar couplings (RDCs) to probe the conformational space populated in solution is demonstrated for the protein BPTI. RDCs allow one to assess accuracy of atomic resolution structures and potentially to characterize low‐populated subspaces corresponding to “excited states” in conformationally labile systems. They also allow one to assess sampling accuracy of molecular dynamics simulations.