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@inproceedings{727774, author = {Macek, Pavel and Novák, Petr and Křížová, Hana and Žídek, Lukáš and Sklenář, Vladimír}, address = {Taiwan}, booktitle = {ISMAR 2007, Program and Abstracts}, keywords = {NMR; relaxation; protein-ligand interactions; internal dynamics; N-15; MD simulations;}, language = {eng}, location = {Taiwan}, note = {pozvaná přednáška}, pages = {63-63}, publisher = {Taiwan Magnetic Resonance Society}, title = {Dynamics of major urinary protein-pheromone interactions: Insight by NMR and MD simulations}, url = {http://ismar2007.sinica.edu.tw/welcome.php}, year = {2007} }
TY - JOUR ID - 727774 AU - Macek, Pavel - Novák, Petr - Křížová, Hana - Žídek, Lukáš - Sklenář, Vladimír PY - 2007 TI - Dynamics of major urinary protein-pheromone interactions: Insight by NMR and MD simulations PB - Taiwan Magnetic Resonance Society CY - Taiwan N1 - pozvaná přednáška KW - NMR KW - relaxation KW - protein-ligand interactions KW - internal dynamics KW - N-15 KW - MD simulations; UR - http://ismar2007.sinica.edu.tw/welcome.php 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 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 -
MACEK, Pavel, Petr NOVÁK, Hana KŘÍŽOVÁ, Lukáš ŽÍDEK a Vladimír SKLENÁŘ. Dynamics of major urinary protein-pheromone interactions: Insight by NMR and MD simulations. In \textit{ISMAR 2007, Program and Abstracts}. Taiwan: Taiwan Magnetic Resonance Society, 2007, s.~63-63.
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