Hydride Transfer in DHFR by Transition Path Sampling, Kinetic Isotope Effects, and Heavy Enzyme Studies
about
Triple Isotope Effects Support Concerted Hydride and Proton Transfer and Promoting Vibrations in Human Heart Lactate DehydrogenaseModulating Enzyme Catalysis through Mutations Designed to Alter Rapid Protein Dynamics.The Effect of Protein Mass Modulation on Human Dihydrofolate Reductase.Examinations of the Chemical Step in Enzyme Catalysis.Rare event simulations reveal subtle key steps in aqueous silicate condensation.Quantifying the limits of transition state theory in enzymatic catalysis.Catalytic-site design for inverse heavy-enzyme isotope effects in human purine nucleoside phosphorylase.Promoting Vibrations and the Function of Enzymes. Emerging Theoretical and Experimental Convergence.
P2860
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P2860
Hydride Transfer in DHFR by Transition Path Sampling, Kinetic Isotope Effects, and Heavy Enzyme Studies
description
2015 nî lūn-bûn
@nan
2015年の論文
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2015年論文
@yue
2015年論文
@zh-hant
2015年論文
@zh-hk
2015年論文
@zh-mo
2015年論文
@zh-tw
2015年论文
@wuu
2015年论文
@zh
2015年论文
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name
Hydride Transfer in DHFR by Tr ...... ects, and Heavy Enzyme Studies
@en
type
label
Hydride Transfer in DHFR by Tr ...... ects, and Heavy Enzyme Studies
@en
prefLabel
Hydride Transfer in DHFR by Tr ...... ects, and Heavy Enzyme Studies
@en
P2093
P2860
P1433
P1476
Hydride Transfer in DHFR by Tr ...... ects, and Heavy Enzyme Studies
@en
P2093
Dimitri Antoniou
Steven D Schwartz
Vern L Schramm
P2860
P304
P356
10.1021/ACS.BIOCHEM.5B01241
P407
P577
2015-12-10T00:00:00Z