Dimethyl sulfoxide binding to globular proteins: a nuclear magnetic relaxation dispersion study.

@article{Jhannesson1997DimethylSB,
  title={Dimethyl sulfoxide binding to globular proteins: a nuclear magnetic relaxation dispersion study.},
  author={Helgi J{\'o}hannesson and Vladimir P. Denisov and Bertil Halle},
  journal={Protein science : a publication of the Protein Society},
  year={1997},
  volume={6 8},
  pages={1756-63}
}
The 2H magnetic relaxation dispersion (NMRD) technique was used to characterize interactions of dimethyl sulfoxide (DMSO) with globular proteins. A difference NMRD experiment involving the N-acetylglucosamine trisaccharide inhibitor, demonstrated that the DMSO 2H NMRD profile in lysozyme solution is due to a single DMSO molecule bound in the active cleft, with a molecular order parameter of 0.47 +/- 0.05 and a residence time in the range 10 ns to 5 ms. With the aid of transverse 2H relaxation… CONTINUE READING