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@inproceedings{708423, author = {Sklenář, Vladimír}, address = {Lubjlana}, booktitle = {Frontieres of Biomolecular NMR}, keywords = {NMR; proteins; dynamics; molecular dynamics; NMR relaxation}, language = {eng}, location = {Lubjlana}, isbn = {961-6104-08-X}, pages = {41-41}, publisher = {Narodna i univerzitetna knjižnica, Ljubljana}, title = {Dynamics of Protein-Ligand Interactions}, year = {2006} }
TY - JOUR ID - 708423 AU - Sklenář, Vladimír PY - 2006 TI - Dynamics of Protein-Ligand Interactions PB - Narodna i univerzitetna knjižnica, Ljubljana CY - Lubjlana SN - 961610408X KW - NMR KW - proteins KW - dynamics KW - molecular dynamics KW - NMR relaxation N2 - Binding of mouse pheromones to major urinary proteins (MUPs) represents a typical example of interactions between lipocalins and their small hydrophobic ligands. Previously, based on the model-free analysis of 15N relaxation data, we observed that the backbone flexibility of MUP-I increased slightly upon pheromone binding, in contrast to the decreased flexibility expected for induced-fit interactions. To shed the light on this unusual observation, we have performed an independent study adopting different methodology. Backbone dynamics of mouse major urinary protein I (MUP-I) was studied by 15N NMR relaxation at multiple temperatures for a complex of MUP-I with its natural pheromonal ligand, 2-sec-4,5-dihydrothiazole, and for the free protein. Graphical analysis of the reduced spectral density values provided an unbiased qualitative picture of the internal motions. Quantitative parameters were obtained using a novel method of simultaneous data fitting at multiple temperatures to several models of different complexity. The relaxation data were complemented by the molecular dynamics simulations. Correlation functions and frequency-dependent order parameters were calculated from the simulated motions of the amide NH vectors. Comparison of the experimental and simulated order parameters and the information about slow conformational exchanges provided a picture of the molecular motions and offered a structural explanation for the observed difference in the dynamics of the free and bound MUP-I. ER -
SKLENÁŘ, Vladimír. Dynamics of Protein-Ligand Interactions. In \textit{Frontieres of Biomolecular NMR}. Lubjlana: Narodna i univerzitetna knjižnica, Ljubljana, 2006, s.~41-41. ISBN~961-6104-08-X.
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