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Calculating protein structures directly from anisotropic spin interaction constraints
Author(s) -
Smurnyy Yegor,
Opella Stanley J.
Publication year - 2006
Publication title -
magnetic resonance in chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.483
H-Index - 72
eISSN - 1097-458X
pISSN - 0749-1581
DOI - 10.1002/mrc.1761
Subject(s) - heteronuclear molecule , chemistry , anisotropy , spin (aerodynamics) , solid state nuclear magnetic resonance , j coupling , dipole , residual dipolar coupling , chemical physics , magnetic dipole–dipole interaction , coupling (piping) , computational chemistry , nuclear magnetic resonance spectroscopy , nuclear magnetic resonance , stereochemistry , physics , quantum mechanics , thermodynamics , organic chemistry , mechanical engineering , engineering
Protein structure determination by solid‐state NMR of aligned samples relies on the fundamental characteristics of the anisotropic nuclear spin interactions present in isotopically labeled proteins. Progress in the implementation of algorithms that calculate protein structures from the orientational constraints in the chemical shift and heteronuclear dipolar coupling interactions is described using both simulated and experimental data. Copyright © 2006 John Wiley & Sons, Ltd.