Detailed Information on Publication Record
2006
Dynamics of Protein-Ligand Interactions
SKLENÁŘ, VladimírBasic information
Original name
Dynamics of Protein-Ligand Interactions
Name in Czech
Dynamika interakcí protein-ligand
Authors
SKLENÁŘ, Vladimír (203 Czech Republic, guarantor)
Edition
Lubjlana, Frontieres of Biomolecular NMR, p. 41-41, 1 pp. 2006
Publisher
Narodna i univerzitetna knjižnica, Ljubljana
Other information
Language
English
Type of outcome
Stať ve sborníku
Field of Study
10600 1.6 Biological sciences
Country of publisher
Slovenia
Confidentiality degree
není předmětem státního či obchodního tajemství
RIV identification code
RIV/00216224:14310/06:00018241
Organization unit
Faculty of Science
ISBN
961-6104-08-X
Keywords in English
NMR; proteins; dynamics; molecular dynamics; NMR relaxation
Tags
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 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.
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 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.
Links
| LC06030, research and development project |
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| MSM0021622413, plan (intention) |
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