Solution-state NMR investigations of triosephosphate isomerase active site loop motion: ligand release in relation to active site loop dynamics
about
Efficient coupling of catalysis and dynamics in the E1 component of Escherichia coli pyruvate dehydrogenase multienzyme complexPredicting functional sites with an automated algorithm suitable for heterogeneous datasetsOptimal alignment for enzymatic proton transfer: structure of the Michaelis complex of triosephosphate isomerase at 1.2-A resolution.Crystal structure of triosephosphate isomerase complexed with 2-phosphoglycolate at 0.83-A resolutionStructure of Plasmodium falciparum triose-phosphate isomerase-2-phosphoglycerate complex at 1.1-A resolutionPerturbation of the Dimer Interface of Triosephosphate Isomerase and its Effect on Trypanosoma cruziNMR and X-ray analysis of structural additivity in metal binding site-swapped hybrids of rubredoxinIncreasing the Conformational Entropy of the Ω-Loop Lid Domain in Phosphoenolpyruvate Carboxykinase Impairs Catalysis and Decreases Catalytic Fidelity,Structural and functional perturbation of Giardia lamblia triosephosphate isomerase by modification of a non-catalytic, non-conserved regionEnzyme Architecture: The Effect of Replacement and Deletion Mutations of Loop 6 on Catalysis by Triosephosphate IsomeraseConnecting Active-Site Loop Conformations and Catalysis in Triosephosphate Isomerase: Insights from a Rare Variation at Residue 96 in the Plasmodial EnzymeEnzyme dynamics from NMR spectroscopyIntrinsic dynamics of an enzyme underlies catalysisReflections on the catalytic power of a TIM-barrel.Nontarget DNA binding shapes the dynamic landscape for enzymatic recognition of DNA damage.Enzymatic catalysis of proton transfer at carbon: activation of triosephosphate isomerase by phosphite dianion.Slow proton transfer from the hydrogen-labelled carboxylic acid side chain (Glu-165) of triosephosphate isomerase to imidazole buffer in D2O.Intrinsic domain and loop dynamics commensurate with catalytic turnover in an induced-fit enzyme.What's in your buffer? Solute altered millisecond motions detected by solution NMR.Triosephosphate isomerase: 15N and 13C chemical shift assignments and conformational change upon ligand binding by magic-angle spinning solid-state NMR spectroscopy.Defining the role of active-site loop fluctuations in dihydrofolate reductase catalysis.Probing the micelle-bound aggregation-prone state of α-synuclein with (19)F NMR spectroscopyTriosephosphate isomerase I170V alters catalytic site, enhances stability and induces pathology in a Drosophila model of TPI deficiency.Network of long-range concerted chemical shift displacements upon ligand binding to human angiogenin.Substrate product equilibrium on a reversible enzyme, triosephosphate isomerase.Interdomain dynamics and coactivation of the mRNA decapping enzyme Dcp2 are mediated by a gatekeeper tryptophan.Substrate-Induced Dimerization of Engineered Monomeric Variants of Triosephosphate Isomerase from Trichomonas vaginalis.Rate and Equilibrium Constants for an Enzyme Conformational Change during Catalysis by Orotidine 5'-Monophosphate DecarboxylaseA Proline-Tryptophan Turn in the Intrinsically Disordered Domain 2 of NS5A Protein Is Essential for Hepatitis C Virus RNA ReplicationEnzyme Tunnels and Gates As Relevant Targets in Drug Design.CADEE: Computer-Aided Directed Evolution of Enzymes.Dynamic requirements for a functional protein hingeRole of Loop-Clamping Side Chains in Catalysis by Triosephosphate Isomerase.The evolutionary origins and catalytic importance of conserved electrostatic networks within TIM-barrel proteins.Effects of cell volume regulating osmolytes on glycerol 3-phosphate binding to triosephosphate isomeraseGates of enzymes.Substrate-driven conformational changes in ClC-ec1 observed by fluorine NMR.Extension of the tryptophan chi2,1 dihedral angle-W3 band frequency relationship to a full rotation: correlations and caveats.Mechanistic Imperatives for Deprotonation of Carbon Catalyzed by Triosephosphate Isomerase: Enzyme-Activation by Phosphite Dianion.A role for flexible loops in enzyme catalysis.
P2860
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P2860
Solution-state NMR investigations of triosephosphate isomerase active site loop motion: ligand release in relation to active site loop dynamics
description
2001 nî lūn-bûn
@nan
2001 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Solution-state NMR investigati ...... n to active site loop dynamics
@ast
Solution-state NMR investigati ...... n to active site loop dynamics
@en
Solution-state NMR investigati ...... n to active site loop dynamics
@nl
type
label
Solution-state NMR investigati ...... n to active site loop dynamics
@ast
Solution-state NMR investigati ...... n to active site loop dynamics
@en
Solution-state NMR investigati ...... n to active site loop dynamics
@nl
prefLabel
Solution-state NMR investigati ...... n to active site loop dynamics
@ast
Solution-state NMR investigati ...... n to active site loop dynamics
@en
Solution-state NMR investigati ...... n to active site loop dynamics
@nl
P2093
P356
P1476
Solution-state NMR investigati ...... n to active site loop dynamics
@en
P2093
P304
P356
10.1006/JMBI.2001.4673
P407
P50
P577
2001-06-29T00:00:00Z