| MACEK, Pavel, Petr NOVÁK, Hana KŘÍŽOVÁ, Lukáš ŽÍDEK and Vladimír SKLENÁŘ. Molecular dynamics study of major urinary protein-pheromone interactions: A structural model for ligand-induced flexibility increase. FEBS Letters. Amsterdam: Elsevier Science B.V., 2006, vol. 580, No 1, p. 682-684. ISSN 0014-5793. |
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@article{701742,
author = {Macek, Pavel and Novák, Petr and Křížová, Hana and Žídek, Lukáš and Sklenář, Vladimír},
article_location = {Amsterdam},
article_number = {1},
keywords = {Major urinary protein; Molecular dynamics simulation; Pheromone–protein interaction; Molecular motion; TZL; Order parameter},
language = {eng},
issn = {0014-5793},
journal = {FEBS Letters},
title = {Molecular dynamics study of major urinary protein-pheromone interactions: A structural model for ligand-induced flexibility increase},
url = {http://dx.doi.org/10.1016/j.febslet.2005.12.088},
volume = {580},
year = {2006}
}
TY - JOUR
ID - 701742
AU - Macek, Pavel - Novák, Petr - Křížová, Hana - Žídek, Lukáš - Sklenář, Vladimír
PY - 2006
TI - Molecular dynamics study of major urinary protein-pheromone interactions: A structural model for ligand-induced flexibility increase
JF - FEBS Letters
VL - 580
IS - 1
SP - 682-684
EP - 682-684
PB - Elsevier Science B.V.
SN - 00145793
KW - Major urinary protein
KW - Molecular dynamics simulation
KW - Pheromone–protein interaction
KW - Molecular motion
KW - TZL
KW - Order parameter
UR - http://dx.doi.org/10.1016/j.febslet.2005.12.088
N2 - Recently, two independent 15N NMR relaxation studies indicated that in contrast to the decreased flexibility expected for induced-fit interactions, the backbone flexibility of major urinary protein isoform I (MUP-I) slightly increased upon complex formation with its natural pheromone 2-sec-butyl-4,5-dihydrothiazol. We have investigated the subtle details of molecular interactions by molecular dynamics simulations in explicit solvent. The calculated order parameters S2 for a free- and ligand-bound protein supply evidence that mobility in various regions of MUP-I can be directly related to small conformational changes of the free- and complexed protein resulting from modifications of the hydrogen bonding network.
ER -
MACEK, Pavel, Petr NOVÁK, Hana KŘÍŽOVÁ, Lukáš ŽÍDEK and Vladimír SKLENÁŘ. Molecular dynamics study of major urinary protein-pheromone interactions: A structural model for ligand-induced flexibility increase. \textit{FEBS Letters}. Amsterdam: Elsevier Science B.V., 2006, vol.~580, No~1, p.~682-684. ISSN~0014-5793.
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