A Comparative Multinuclear Relaxation Study of Protein-DMSO and Protein-Water Interactions

✍ Scribed by B.P. Hills; F.A. Favret

• Book ID: 102972423
• Publisher: Elsevier Science
• Year: 1994
• Tongue: English
• Weight: 785 KB
• Volume: 103
• Category: Article
• ISSN: 1064-1866
• DOI: 10.1006/jmrb.1994.1022

✦ Synopsis

A comparative multinuclear relaxation study of DMSO-protein and water-protein interactions has been undertaken to discover whether cross relaxation between water and protein protons proceeds mainly by proton-exchange or direct dipolar interactions. The analysis suggests that the proton-exchange mechanism dominates the cross relaxation from water. In contrast, the high efficiency of dipolar cross relaxation in DMSOprotein gels, which lack exchangeable protons, arises from an unusually long lifetime of DMSO molecules at the protein interface. These results are important for understanding the origin of image contrast in clinical nuclear magnetic resonance imaging and the nature of protein-solvent interactions in nonaqueous Systems. & 1994 Academic Press. Inc.