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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Jóhannesson, H. Denisov, V. P. Halle, B. |
| Description | Country affiliation: Sweden Author Affiliation: Jóhannesson H ( Condensed Master Magnetic Resonance Group, Department of Chemistry, Lund University, Sweden. haukur.johannesson@fkem2.lth.se) |
| Abstract | 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 data, the upper bound of the residence time was further reduced to 100 microns. A 1H shift titration experiment was also performed, yielding a binding constant of 2.3 +/- 0.3 M-1 at 27 degrees C. In contrast to lysozyme, no DMSO dispersion was observed for bovine pancreatic trypsin inhibitor (BPTI), indicating that a stable DMSO-protein complex requires a cleft of appropriate geometry in addition to hydrogen-bond and hydrophobic interactions. |
| ISSN | 09618368 |
| e-ISSN | 1469896X |
| Journal | Protein Science |
| Issue Number | 8 |
| Volume Number | 6 |
| Language | English |
| Publisher | Wiley-Blackwell (on behalf of The Protein Society) |
| Publisher Date | 1997-08-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Aprotinin Metabolism Dimethyl Sulfoxide Muramidase Chemistry Deuterium Magnetic Resonance Spectroscopy Oligosaccharides Protein Conformation Research Support, Non-u.s. Gov't Discipline Biochemistry |
| Content Type | Text |
| Resource Type | Article |
| Subject | Medicine Molecular Biology Biochemistry |
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