The 2.0-A resolution structure of Escherichia coli histidine-containing phosphocarrier protein HPr. A redetermination
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X-ray structure of HPr kinase: a bacterial protein kinase with a P-loop nucleotide-binding domainA restraint molecular dynamics and simulated annealing approach for protein homology modeling utilizing mean anglesSolution structure of the phosphoryl transfer complex between the signal transducing proteins HPr and IIAGlucose of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase systemThermodynamic and structural characterization of Asn and Ala residues in the disallowed II′ region of the Ramachandran plotStructural Investigation of a Phosphorylation-Catalyzed, Isoaspartate-Free, Protein Succinimide: Crystallographic Structure of Post-Succinimide His15Asp Histidine-Containing Protein † ‡Solution Structure of the IIAChitobiose-IIBChitobiose Complex of the N,N'-Diacetylchitobiose Branch of the Escherichia coli Phosphotransferase SystemSolution Structure of the IIAChitobiose-HPr Complex of the N,N'-Diacetylchitobiose Branch of the Escherichia coli Phosphotransferase SystemAccurate and rapid docking of protein-protein complexes on the basis of intermolecular nuclear overhauser enhancement data and dipolar couplings by rigid body minimizationUsing the experimentally determined components of the overall rotational diffusion tensor to restrain molecular shape and size in NMR structure determination of globular proteins and protein-protein complexes.Predicting interaction sites from the energetics of isolated proteins: a new approach to epitope mapping.A novel approach for assessing macromolecular complexes combining soft-docking calculations with NMR data.Emergence of protein fold families through rational designVisualizing lowly-populated regions of the free energy landscape of macromolecular complexes by paramagnetic relaxation enhancementDirect use of 15N relaxation rates as experimental restraints on molecular shape and orientation for docking of protein-protein complexes.Structure, dynamics and biophysics of the cytoplasmic protein-protein complexes of the bacterial phosphoenolpyruvate: sugar phosphotransferase system.Solution NMR structure of the 48-kDa IIAMannose-HPr complex of the Escherichia coli mannose phosphotransferase systemIdentification of a site in the phosphocarrier protein, HPr, which influences its interactions with sugar permeases of the bacterial phosphotransferase system: kinetic analyses employing site-specific mutants.Impact of phosphorylation on structure and thermodynamics of the interaction between the N-terminal domain of enzyme I and the histidine phosphocarrier protein of the bacterial phosphotransferase systemPhosphorylation-induced torsion-angle strain in the active center of HPr, detected by NMR and restrained molecular dynamics refinement.Probing the protein-folding mechanism using denaturant and temperature effects on rate constantsElectrostatics in protein-protein docking.High-resolution structure of the histidine-containing phosphocarrier protein (HPr) from Staphylococcus aureus and characterization of its interaction with the bifunctional HPr kinase/phosphorylase.Defining the epitope region of a peptide from the Streptomyces coelicolor phosphoenolpyruvate:sugar phosphotransferase system able to bind to the enzyme IPhosphorylation on histidine is accompanied by localized structural changes in the phosphocarrier protein, HPr from Bacillus subtilis.Robust structure-based resonance assignment for functional protein studies by NMR.Single-molecule protein unfolding in solid state nanopores.Conformational stability of HPr: the histidine-containing phosphocarrier protein from Bacillus subtilisInvestigation of a side-chain-side-chain hydrogen bond by mutagenesis, thermodynamics, and NMR spectroscopySorting the chaff from the wheat at the PDB.Structure of the NPr:EINNtr Complex: Mechanism for Specificity in Paralogous Phosphotransferase Systems.
P2860
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P2860
The 2.0-A resolution structure of Escherichia coli histidine-containing phosphocarrier protein HPr. A redetermination
description
1993 nî lūn-bûn
@nan
1993 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1993 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
name
The 2.0-A resolution structure ...... protein HPr. A redetermination
@ast
The 2.0-A resolution structure ...... protein HPr. A redetermination
@en
The 2.0-A resolution structure ...... protein HPr. A redetermination
@nl
type
label
The 2.0-A resolution structure ...... protein HPr. A redetermination
@ast
The 2.0-A resolution structure ...... protein HPr. A redetermination
@en
The 2.0-A resolution structure ...... protein HPr. A redetermination
@nl
prefLabel
The 2.0-A resolution structure ...... protein HPr. A redetermination
@ast
The 2.0-A resolution structure ...... protein HPr. A redetermination
@en
The 2.0-A resolution structure ...... protein HPr. A redetermination
@nl
P2093
P1476
The 2.0-A resolution structure ...... protein HPr. A redetermination
@en
P2093
P304
P407
P577
1993-10-25T00:00:00Z