Application of solid-state NMR restraint potentials in membrane protein modeling.
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ABSTRACT:
SUBMITTER: Lee J
PROVIDER: S-EPMC2546517 | biostudies-literature | 2008 Jul
REPOSITORIES: biostudies-literature
Publications
Application of solid-state NMR restraint potentials in membrane protein modeling.
Lee Jinhyuk J Chen Jianhan J Brooks Charles L CL Im Wonpil W
Journal of magnetic resonance (San Diego, Calif. : 1997) 20080418 1
We have developed a set of orientational restraint potentials for solid-state NMR observables including (15)N chemical shift and (15)N-(1)H dipolar coupling. Torsion angle molecular dynamics simulations with available experimental (15)N chemical shift and (15)N-(1)H dipolar coupling as target values have been performed to determine orientational information of four membrane proteins and to model the structures of some of these systems in oligomer states. The results suggest that incorporation of ...[more]
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