Closed conformation of the active site loop of rabbit muscle triosephosphate isomerase in the absence of substrate: evidence of conformational heterogeneity

Closed conformation of the active site loop of rabbit muscle triosephosphate isomerase in the absence of substrate: evidence of conformational heterogeneity

Item
http://www.wikidata.org/entity/Q27642652
Cooperativity in monomeric enzymes with single ligand-binding sitesStructural and functional perturbation of Giardia lamblia triosephosphate isomerase by modification of a non-catalytic, non-conserved regionGalaxyWEB server for protein structure prediction and refinement.Slow proton transfer from the hydrogen-labelled carboxylic acid side chain (Glu-165) of triosephosphate isomerase to imidazole buffer in D2O.Gated binding of ligands to HIV-1 protease: Brownian dynamics simulations in a coarse-grained model.Ionic strength dependence of F-actin and glycolytic enzyme associations: a Brownian dynamics simulations approach.Substrate-Induced Dimerization of Engineered Monomeric Variants of Triosephosphate Isomerase from Trichomonas vaginalis.Ion Mobility-Mass Spectrometry Analysis of Cross-Linked Intact Multiprotein Complexes: Enhanced Gas-Phase Stabilities and Altered Dissociation Pathways.Inhibition of triosephosphate isomerase by phosphoenolpyruvate in the feedback-regulation of glycolysis.BD SIMULATIONS OF THE IONIC STRENGTH DEPENDENCE OF THE INTERACTIONS BETWEEN TRIOSE PHOSPHATE ISOMERASE AND F-ACTIN.Biopharmaceutical Informatics: supporting biologic drug development via molecular modelling and informatics.A novel inhibitor of Mammalian triosephosphate isomerase found by an in silico approach.Expression, purification, crystallization and preliminary X-ray diffraction studies of triosephosphate isomerase from methicillin-resistant Staphylococcus aureus (MRSA252).Long-lived conformational isomerism of protein dimers: the role of the free energy of subunit association.Detection of the protein dimers, multiple monomeric states and hydrated forms of Plasmodium falciparum triosephosphate isomerase in the gas phase.
P2860

Closed conformation of the active site loop of rabbit muscle triosephosphate isomerase in the absence of substrate: evidence of conformational heterogeneity

Item
http://www.wikidata.org/entity/Q27642652
description
2003 nî lūn-bûn
@nan
2003 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2003年の論文
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2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
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name
Closed conformation of the act ...... f conformational heterogeneity
@ast
Closed conformation of the act ...... f conformational heterogeneity
@en
Closed conformation of the act ...... f conformational heterogeneity
@nl
type
label
Closed conformation of the act ...... f conformational heterogeneity
@ast
Closed conformation of the act ...... f conformational heterogeneity
@en
Closed conformation of the act ...... f conformational heterogeneity
@nl
prefLabel
Closed conformation of the act ...... f conformational heterogeneity
@ast
Closed conformation of the act ...... f conformational heterogeneity
@en
Closed conformation of the act ...... f conformational heterogeneity
@nl
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P1476
P2093
P304
P31
P356
P407
P433
P478
P577
P698
P356
P1433
P1476
Closed conformation of the act ...... f conformational heterogeneity
@en
P2093
P304
P31
P356
P407
P433
P478
P577
P698