Confirmation of the assignment of the low-field proton resonance of serine proteases by using specifically nitrogen-15 labeled enzyme.
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Inhibitor binding induces active site stabilization of the HCV NS3 protein serine protease domainUnconventional serine proteases: variations on the catalytic Ser/His/Asp triad configurationEnergy considerations show that low-barrier hydrogen bonds do not offer a catalytic advantage over ordinary hydrogen bondsUnusual 1H NMR chemical shifts support (His) C(epsilon) 1...O==C H-bond: proposal for reaction-driven ring flip mechanism in serine protease catalysis.Proton bridging in the interactions of thrombin with small inhibitorsLocating active-site hydrogen atoms in D-xylose isomerase: time-of-flight neutron diffractionCatalytic reaction mechanism of acetylcholinesterase determined by Born-Oppenheimer ab initio QM/MM molecular dynamics simulations.Specific Inter-residue Interactions as Determinants of Human Monoacylglycerol Lipase Catalytic Competency: A ROLE FOR GLOBAL CONFORMATIONAL CHANGES.Biosynthetic incorporation of 15N and 13C for assignment and interpretation of nuclear magnetic resonance spectra of proteins.Quantum mechanical modeling: a tool for the understanding of enzyme reactions.Proton-detected heteronuclear edited and correlated nuclear magnetic resonance and nuclear Overhauser effect in solution.Determination of the ionization state of the active-site histidine in a subtilisin-(chloromethane inhibitor) derivative by 13C-NMR.NMR studies of the hydrogen bonds involving the catalytic triad of Escherichia coli thioesterase/protease I.pH-dependent random coil (1)H, (13)C, and (15)N chemical shifts of the ionizable amino acids: a guide for protein pK a measurements.Connecting Classical QSAR and LERE Analyses Using Modern Molecular Calculations, LERE-QSAR (VI): Hydrolysis of Substituted Hippuric Acid Phenyl Esters by Trypsin.13C and1H NMR Studies of Ionizations and Hydrogen Bonding in Chymotrypsin-Glyoxal Inhibitor Complexes
P2860
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P2860
Confirmation of the assignment of the low-field proton resonance of serine proteases by using specifically nitrogen-15 labeled enzyme.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on December 1985
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Confirmation of the assignment ...... ly nitrogen-15 labeled enzyme.
@en
Confirmation of the assignment ...... ly nitrogen-15 labeled enzyme.
@nl
type
label
Confirmation of the assignment ...... ly nitrogen-15 labeled enzyme.
@en
Confirmation of the assignment ...... ly nitrogen-15 labeled enzyme.
@nl
prefLabel
Confirmation of the assignment ...... ly nitrogen-15 labeled enzyme.
@en
Confirmation of the assignment ...... ly nitrogen-15 labeled enzyme.
@nl
P2860
P356
P1476
Confirmation of the assignment ...... ly nitrogen-15 labeled enzyme.
@en
P2093
W W Bachovchin
P2860
P304
P356
10.1073/PNAS.82.23.7948
P407
P577
1985-12-01T00:00:00Z