MACEK, Pavel, Petr NOVÁK, Hana KŘÍŽOVÁ, Lukáš ŽÍDEK and Vladimír SKLENÁŘ. Dynamics of major urinary protein-pheromone interactions: Insight by NMR and MD simulations. In ISMAR 2007, Program and Abstracts. Taiwan: Taiwan Magnetic Resonance Society, 2007, p. 63-63.
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Basic information
Original name Dynamics of major urinary protein-pheromone interactions: Insight by NMR and MD simulations
Name in Czech Dynamika interakce močovinového proteinu s feromonem: Studie pomocí NMR spektroskopie a MD simulací.
Authors MACEK, Pavel (203 Czech Republic), Petr NOVÁK (203 Czech Republic), Hana KŘÍŽOVÁ (203 Czech Republic), Lukáš ŽÍDEK (203 Czech Republic) and Vladimír SKLENÁŘ (203 Czech Republic, guarantor).
Edition Taiwan, ISMAR 2007, Program and Abstracts, p. 63-63, 1 pp. 2007.
Publisher Taiwan Magnetic Resonance Society
Other information
Original language English
Type of outcome Proceedings paper
Field of Study 10610 Biophysics
Country of publisher Taiwan
Confidentiality degree is not subject to a state or trade secret
WWW URL
RIV identification code RIV/00216224:14310/07:00022902
Organization unit Faculty of Science
Keywords in English NMR; relaxation; protein-ligand interactions; internal dynamics; N-15; MD simulations;
Tags internal dynamics, MD simulations, N-15, NMR, protein-ligand interactions, relaxation
Tags International impact
Changed by Changed by: prof. RNDr. Vladimír Sklenář, DrSc., učo 2611. Changed: 20/6/2008 12:55.
Abstract
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.
Abstract (in Czech)
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.
Links
LC06030, research and development projectName: Biomolekulární centrum
Investor: Ministry of Education, Youth and Sports of the CR, Biomolecular centre
MSM0021622413, plan (intention)Name: Proteiny v metabolismu a při interakci organismů s prostředím
Investor: Ministry of Education, Youth and Sports of the CR, Proteins in metabolism and interaction of organisms with the environment
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