Detailed Information on Publication Record
2007
Dynamics of major urinary protein-pheromone interactions: Insight by NMR and MD simulations
MACEK, Pavel, Petr NOVÁK, Hana KŘÍŽOVÁ, Lukáš ŽÍDEK, Vladimír SKLENÁŘ et. al.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
Language
English
Type of outcome
Stať ve sborníku
Field of Study
10610 Biophysics
Country of publisher
Taiwan
Confidentiality degree
není předmětem státního či obchodního tajemství
References:
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
International impact
Změněno: 20/6/2008 12:55, prof. RNDr. Vladimír Sklenář, DrSc.
V originále
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.
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 project |
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| MSM0021622413, plan (intention) |
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