Dresden 2003 – wissenschaftliches Programm

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CPP: Chemische Physik und Polymerphysik

CPP 21: POSTER B

CPP 21.7: Poster

Dienstag, 25. März 2003, 19:00–21:00, ZEU/250

¹⁷O NMR INVESTIGATION OF PROTEIN-WATER INTERACTION — •Maciej Krzystyniak¹, Judith Albrecht², and Gerd Buntkowsky² — ¹Institute of Experimental Physics, Free University of Berlin, D-14195 Berlin, Germany — ²Insitute of Chemistry,Free University of Berlin, D-14195 Berlin, Germany

It is generally assumed that water, in the presence of macromolecules, is composed of three phases: free water, whose properties are similar to pure water, water weakly bound, or vicinal water, whose physical properties are different from both the solid and liquid states; and water bound to macromolecules. The fluctuations of water relaxation observed by ¹H NMR are difficult to interpret, as the effects of proton exchange, cross-relaxation and hindered water rotation tend to modify the water relaxation properties simultaneously. As ¹⁷O NMR is free of such problems, the studies of ¹⁷O NMR permit the selective analysis of the effect of reorientationally hindered water on the overall relaxation process. In the present work, we present the results of the ¹⁷O NMR study of the BSA water solution. Longitudinal and transversal relaxation times were measured for different protein concentrations aiming at the determination of the fraction of the surface bound water molecules and their rotational correlation time.