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Validating the use of database potentials in protein structure determination by NMR
Author(s) -
Mertens Haydyn D.T.,
Gooley Paul R.
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.09.017
Subject(s) - ramachandran plot , residual dipolar coupling , residual , protein structure , nuclear magnetic resonance spectroscopy , chemistry , dipole , quality (philosophy) , biological system , crystallography , computer science , physics , algorithm , biology , biochemistry , stereochemistry , quantum mechanics , organic chemistry
The refinement of protein structures determined by nuclear magnetic resonance spectroscopy against database potentials of mean force allows for the exclusion of unfavourable conformations of the protein backbone during a structure calculation, resulting in protein structures with a marked improvement in Ramachandran statistics. In this communication, we use multiple sets of residual dipolar couplings as quality assessment criteria for several proteins and show that not only do the Ramachandran and structural quality statistics improve, but a significant improvement in the accuracy of structures is achieved upon refinement.