2006
Dynamics of Protein-Ligand Interactions
SKLENÁŘ, VladimírZákladní údaje
Originální název
Dynamics of Protein-Ligand Interactions
Název česky
Dynamika interakcí protein-ligand
Autoři
SKLENÁŘ, Vladimír (203 Česká republika, garant)
Vydání
Lubjlana, Frontieres of Biomolecular NMR, od s. 41-41, 1 s. 2006
Nakladatel
Narodna i univerzitetna knjižnica, Ljubljana
Další údaje
Jazyk
angličtina
Typ výsledku
Stať ve sborníku
Obor
10600 1.6 Biological sciences
Stát vydavatele
Slovinsko
Utajení
není předmětem státního či obchodního tajemství
Kód RIV
RIV/00216224:14310/06:00018241
Organizační jednotka
Přírodovědecká fakulta
ISBN
961-6104-08-X
Klíčová slova anglicky
NMR; proteins; dynamics; molecular dynamics; NMR relaxation
Štítky
Příznaky
Mezinárodní význam
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.
Česky
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.
Návaznosti
| LC06030, projekt VaV |
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| MSM0021622413, záměr |
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