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- W2001764778 abstract "Abstract 13C nuclear spin relaxation times (T1 and T2) were measured for three glycine α-carbon atoms in aqueous staphylococcal nuclease. Three forms of the protein were studied: the uncomplexed nuclease, its calcium complex, and a ternary complex with calcium and an inhibitor. The NMR data were used to calculate order parameters and effective correlation times that describe internal motion. Major sources of experimental error were identified, and statistical analyses were used to examine the accuracy of the method. Results showed that when the inhibitor binds to the protein, a significant increase in stiffness occurs at glycines near the calcium binding site." @default.
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- W2001764778 date "1988-11-01" @default.
- W2001764778 modified "2023-09-26" @default.
- W2001764778 title "NMR relaxation study of internal motions in Staphylococcal nuclease" @default.
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- W2001764778 doi "https://doi.org/10.1016/0022-2364(88)90298-3" @default.
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