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Molecular dynamics simulations reveal proton transfer pathways in cytochrome C-dependent nitric oxide reductaseStructural insights into electron transfer in caa3-type cytochrome oxidaseCrystal structure of quinol-dependent nitric oxide reductase from Geobacillus stearothermophilusMolecular basis of RNA guanine-7 methyltransferase (RNMT) activation by RAM.Electrostatic basis for the unidirectionality of the primary proton transfer in cytochrome c oxidase.Enzyme millisecond conformational dynamics do not catalyze the chemical step.The barrier for proton transport in aquaporins as a challenge for electrostatic models: the role of protein relaxation in mutational calculations.Polarizable Force Fields: History, Test Cases, and Prospects.The energetics of the primary proton transfer in bacteriorhodopsin revisited: it is a sequential light-induced charge separation after allTwo-dimensional optical three-pulse photon echo spectroscopy. I. Nonperturbative approach to the calculation of spectra.Two-dimensional optical three-pulse photon echo spectroscopy. II. Signatures of coherent electronic motion and exciton population transfer in dimer two-dimensional spectra.Intracellular Transfer of Na+ in an Active-State G-Protein-Coupled Receptor.On the role of subunit M in cytochrome cbb3 oxidase.Insights into proton translocation in cbb3 oxidase from MD simulations.Transient Phenomena in Time- and Frequency-Gated Spontaneous EmissionLysyl-tRNA synthetase as a drug target in malaria and cryptosporidiosisMechanism of allosteric activation of human mRNA cap methyltransferase (RNMT) by RAM: insights from accelerated molecular dynamics simulations
P50
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P50
description
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Andrei V Pisliakov
@ast
Andrei V Pisliakov
@en
Andrei V Pisliakov
@es
Andrei V Pisliakov
@nl
type
label
Andrei V Pisliakov
@ast
Andrei V Pisliakov
@en
Andrei V Pisliakov
@es
Andrei V Pisliakov
@nl
prefLabel
Andrei V Pisliakov
@ast
Andrei V Pisliakov
@en
Andrei V Pisliakov
@es
Andrei V Pisliakov
@nl
P106
P1153
7801331302
P21
P31
P496
0000-0003-1536-0589