Contributions to protein entropy and heat capacity from bond vector motions measured by NMR spin relaxation.

@article{Yang1997ContributionsTP,
  title={Contributions to protein entropy and heat capacity from bond vector motions measured by NMR spin relaxation.},
  author={D S Yang and Y K Mok and Julie Deborah Forman-Kay and Neil A. Farrow and Lewis E. Kay},
  journal={Journal of molecular biology},
  year={1997},
  volume={272 5},
  pages={790-804}
}
The backbone dynamics of both folded and unfolded states of staphylococcal nuclease (SNase) and the N-terminal SH3 domain from drk (drkN SH3) are studied at two different temperatures. A simple method for obtaining order parameters, describing the amplitudes of motion of bond vectors, from NMR relaxation measurements of both folded and unfolded proteins is presented and the data obtained for 15N-NH bond vectors in both the SNase and drkN SH3 systems analyzed with this approach. Using a recently… CONTINUE READING

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