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Dynamics in aqueous solutions of the pentasaccharide corresponding to the binding site of heparin for antithrombin III studied by NMR relaxation measurements by Miloš Hricovíni; Giangiacomo Torri is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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1H NMR and 13C NMR relaxation measurements at different magnetic field strengths were used to study the nature of overall and internal motions, in aqueous solution, of the synthetic pentasaccharide (A-G-A\*-I-A M) corresponding to the binding site of heparin for antithrombin III. Two-dimensional double INEPT spectra were recorded at 11.7 T with and without suppression of cross-correlation effects between dipolar and chemical shift anisotropy relaxation mechanisms in measurements of spin-lattice and spin-spin relaxation times. Moreover, longitudinal relaxation times were collected at 7 T with the inversion recovery method. One dimensional NOESY spectra were recorded at 11.7 T and 9.4 T with various mixing times when spins of the AI\* and A4\* protons were inverted in the central residue of the pentasaccharide. Differences in the T~ relaxation times, as well as in the cross-relaxation rates between protons relaxing through fixed distances in the A\* residue, indicated that the molecule tumbles anisotropically in solution. However, in order to achieve agreement between the spectral and the model data, the presence of internal motions had to be also considered, in addition to the assum

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Author

Miloš Hricovíni; Giangiacomo Torri

Publisher

Elsevier Science; Elsevier ; Elsevier Ltd.; Elsevier BV (ISSN 0008-6215)

Published

1995

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)