Role of loop-loop interactions in coordinating motions and enzymatic function in triosephosphate isomerase.
about
Identification and analysis of residues contained on β → α loops of the dual-substrate (βα)8phosphoribosyl isomerase A specific for its phosphoribosyl anthranilate isomerase activityHigh resolution crystal structures of triosephosphate isomerase complexed with its suicide inhibitors: The conformational flexibility of the catalytic glutamate in its closed, liganded active siteRevisiting the mechanism of the triosephosphate isomerase reaction: the role of the fully conserved glutamic acid 97 residueStructural and functional perturbation of Giardia lamblia triosephosphate isomerase by modification of a non-catalytic, non-conserved regionAlternative splice variants in TIM barrel proteins from human genome correlate with the structural and evolutionary modularity of this versatile protein foldStructural and functional importance of local and global conformational fluctuations in the RNase A superfamily.Solution conformation and dynamics of the HIV-1 integrase core domain.An introduction to NMR-based approaches for measuring protein dynamics.Rate-limiting domain and loop motions in arginine kinasePredicting flexible loop regions that interact with ligands: the challenge of accurate scoringRole of Loop-Clamping Side Chains in Catalysis by Triosephosphate Isomerase.Gates of enzymes.Structural mutations that probe the interactions between the catalytic and dianion activation sites of triosephosphate isomerase.A distal mutation perturbs dynamic amino acid networks in dihydrofolate reductase.Mechanistic Imperatives for Deprotonation of Carbon Catalyzed by Triosephosphate Isomerase: Enzyme-Activation by Phosphite Dianion.Enzyme architecture: remarkably similar transition states for triosephosphate isomerase-catalyzed reactions of the whole substrate and the substrate in piecesA role for flexible loops in enzyme catalysis.A guide to the effects of a large portion of the residues of triosephosphate isomerase on catalysis, stability, druggability, and human disease.The critical role of the loops of triosephosphate isomerase for its oligomerization, dynamics, and functionality.Probing local structural fluctuations in myoglobin by size-dependent thiol-disulfide exchangeSpecies-Specific Inactivation of Triosephosphate Isomerase from Trypanosoma brucei: Kinetic and Molecular Dynamics Studies.Enzyme Architecture: Amino Acid Side-Chains That Function To Optimize the Basicity of the Active Site Glutamate of Triosephosphate Isomerase
P2860
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P2860
Role of loop-loop interactions in coordinating motions and enzymatic function in triosephosphate isomerase.
description
2009 nî lūn-bûn
@nan
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
2009年论文
@zh
2009年论文
@zh-cn
name
Role of loop-loop interactions ...... in triosephosphate isomerase.
@en
Role of loop-loop interactions ...... in triosephosphate isomerase.
@nl
type
label
Role of loop-loop interactions ...... in triosephosphate isomerase.
@en
Role of loop-loop interactions ...... in triosephosphate isomerase.
@nl
prefLabel
Role of loop-loop interactions ...... in triosephosphate isomerase.
@en
Role of loop-loop interactions ...... in triosephosphate isomerase.
@nl
P2860
P356
P1433
P1476
Role of loop-loop interactions ...... n in triosephosphate isomerase
@en
P2093
J Patrick Loria
P2860
P304
P356
10.1021/BI9002887
P407
P577
2009-06-01T00:00:00Z