Synergy of molecular dynamics and isothermal titration calorimetry in studies of Allostery

0373140 - ÚVGZ 2012 RIV US eng J - Článek v odborném periodiku
Strawn, R. - Stockner, T. - Melicherčík, Milan - Jin, L. - Xue,, W. F. - Carey, J. - Ettrich, Rüdiger
Synergy of molecular dynamics and isothermal titration calorimetry in studies of Allostery.
Methods in Enzymology. Roč. 492, - (2011), s. 151-188. ISSN 0076-6879
Grant CEP: GA MŠMT(CZ) LC06010; GA ČR GAP207/10/1934
Výzkumný záměr: CEZ:AV0Z60870520
Klíčová slova: hexameric arginine repressor * DNA-binding domain * escherichia-coli * ligand-binding * bacillus-stearothhermophilus * proteins * systems * model * simulations * operator
Kód oboru RIV: EH - Ekologie - společenstva
Impakt faktor: 2.042, rok: 2011

Despite decades of intensive study, allosteric effects have eluded an intellectually satisfying integrated understanding that includes a description of the reaction coordinate in terms of species distributions of structures and free energy levels in the conformational ensemble. This chapter illustrates a way to fill this gap by interpreting thermodynamic and structural results through the lens of molecular dynamics simulation analysis to link atomic-level detail with global response. In this synergistic approach molecular dynamics forms an integral part of a feedback loop of hypothesis, experimental design, and interpretation that conforms to the scientific method.
Trvalý link: http://hdl.handle.net/11104/0206295