Different dynamical effects in mesophilic and hyperthermophilic dihydrofolate reductases.
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The importance of ensemble averaging in enzyme kineticsChemical Ligation and Isotope Labeling to Locate Dynamic Effects during Catalysis by Dihydrofolate ReductasePinpointing dynamic coupling in enzymes for efficient drug design.Halophilic mechanism of the enzymatic function of a moderately halophilic dihydrofolate reductase from Haloarcula japonica strain TR-1.Isotope Substitution of Promiscuous Alcohol Dehydrogenase Reveals the Origin of Substrate Preference in the Transition State.Protein motions and dynamic effects in enzyme catalysis.Minimization of dynamic effects in the evolution of dihydrofolate reductase† †Electronic supplementary information (ESI) available: Full experimental procedures; mass spectra of purified proteins; circular dichroism spectra, tabulated experimental d
P2860
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P2860
Different dynamical effects in mesophilic and hyperthermophilic dihydrofolate reductases.
description
2014 nî lūn-bûn
@nan
2014年の論文
@ja
2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
2014年论文
@zh
2014年论文
@zh-cn
name
Different dynamical effects in mesophilic and hyperthermophilic dihydrofolate reductases.
@en
type
label
Different dynamical effects in mesophilic and hyperthermophilic dihydrofolate reductases.
@en
prefLabel
Different dynamical effects in mesophilic and hyperthermophilic dihydrofolate reductases.
@en
P2860
P356
P1476
Different dynamical effects in mesophilic and hyperthermophilic dihydrofolate reductases
@en
P2093
Rudolf K Allemann
P2860
P304
P356
10.1021/JA502673H
P407
P577
2014-05-05T00:00:00Z