Increasing the time step with mass scaling in Born-Oppenheimer ab initio QM/MM molecular dynamics simulations. - Wikidata - awgldk - TriplyDB

Increasing the time step with mass scaling in Born-Oppenheimer ab initio QM/MM molecular dynamics simulations.

Increasing the time step with mass scaling in Born-Oppenheimer ab initio QM/MM molecular dynamics simulations.

http://www.wikidata.org/entity/Q37411723

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Catalytic reaction mechanism of acetylcholinesterase determined by Born-Oppenheimer ab initio QM/MM molecular dynamics simulations.Computational enzymatic catalysis--clarifying enzymatic mechanisms with the help of computers.Aging mechanism of soman inhibited acetylcholinesterase.A proton-shuttle reaction mechanism for histone deacetylase 8 and the catalytic role of metal ions Thiol versus hydroxamate as zinc binding group in HDAC inhibition: An ab initio QM/MM molecular dynamics study.Low-mass molecular dynamics simulation for configurational sampling enhancement: More evidence and theoretical explanation.On the use of mass scaling for stable and efficient simulated tempering with molecular dynamics.Mass-scaling replica-exchange molecular dynamics optimizes computational resources with simpler algorithm.

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Increasing the time step with mass scaling in Born-Oppenheimer ab initio QM/MM molecular dynamics simulations.

http://www.wikidata.org/entity/Q37411723

description

article científic

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article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on December 2009

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vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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name

Increasing the time step with ...... olecular dynamics simulations.

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Increasing the time step with ...... olecular dynamics simulations.

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Increasing the time step with ...... olecular dynamics simulations.

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Increasing the time step with ...... olecular dynamics simulations.

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Increasing the time step with ...... olecular dynamics simulations.

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Increasing the time step with ...... olecular dynamics simulations.

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Journal of Computational Chemistry

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Increasing the time step with ...... olecular dynamics simulations.

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Han Zheng

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Shenglong Wang

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Yingkai Zhang

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P2860

Structure and catalytic mechanism of a SET domain protein methyltransferase

Theoretical studies of enzymic reactions: dielectric, electrostatic and steric stabilization of the carbonium ion in the reaction of lysozyme

Quantum mechanical methods for enzyme kinetics.

Structure/function correlations of proteins using MM, QM/MM, and related approaches: methods, concepts, pitfalls, and current progress.

Catalysis and specificity in enzymes: a study of triosephosphate isomerase and comparison with methyl glyoxal synthase.

Ab initio quantum chemical and mixed quantum mechanics/molecular mechanics (QM/MM) methods for studying enzymatic catalysis.

Modelling enzyme reaction mechanisms, specificity and catalysis.

Ab initio quantum mechanical/molecular mechanical molecular dynamics simulation of enzyme catalysis: the case of histone lysine methyltransferase SET7/9.

Free energies of chemical reactions in solution and in enzymes with ab initio quantum mechanics/molecular mechanics methods

How do SET-domain protein lysine methyltransferases achieve the methylation state specificity? Revisited by Ab initio QM/MM molecular dynamics simulations.

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2706-2711

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scholarly article

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10.1002/JCC.21296

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16

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30

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19399770

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