Conformational stability of HPr: the histidine-containing phosphocarrier protein from Bacillus subtilis - Wikidata - awgldk - TriplyDB

Conformational stability of HPr: the histidine-containing phosphocarrier protein from Bacillus subtilis

Conformational stability of HPr: the histidine-containing phosphocarrier protein from Bacillus subtilis

http://www.wikidata.org/entity/Q42123512

about

Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding A direct comparison of helix propensity in proteins and peptides.Helix is a helix is a helix?BPPred: a Web-based computational tool for predicting biophysical parameters of proteins.Equilibrium constants and free energies in unfolding of proteins in urea solutions Phosphorylation of serine-46 in HPr, a key regulatory protein in bacteria, results in stabilization of its solution structure.Heat capacity change for ribonuclease A folding.Practical approaches to protein folding and assembly: spectroscopic strategies in thermodynamics and kinetics.Investigation of a side-chain-side-chain hydrogen bond by mutagenesis, thermodynamics, and NMR spectroscopy The histidine-phosphocarrier protein of Streptomyces coelicolor folds by a partially folded species at low pH.The conformational stability of the Streptomyces coelicolor histidine-phosphocarrier protein. Characterization of cold denaturation and urea-protein interactions.Determining the conformational stability of a protein from urea and thermal unfolding curves.Fusion with anticodon binding domain of GluRS is not sufficient to alter the substrate specificity of a chimeric Glu-Q-RS.

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P2860

Conformational stability of HPr: the histidine-containing phosphocarrier protein from Bacillus subtilis

http://www.wikidata.org/entity/Q42123512

description

1995 nî lūn-bûn

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1995年の論文

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1995年論文

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1995年論文

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1995年論文

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1995年論文

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1995年論文

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1995年论文

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1995年论文

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1995年论文

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name

Conformational stability of HP ...... protein from Bacillus subtilis

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Conformational stability of HP ...... protein from Bacillus subtilis

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type

label

Conformational stability of HP ...... protein from Bacillus subtilis

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Conformational stability of HP ...... protein from Bacillus subtilis

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prefLabel

Conformational stability of HP ...... protein from Bacillus subtilis

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Conformational stability of HP ...... protein from Bacillus subtilis

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Protein Science

P1476

Conformational stability of HP ...... protein from Bacillus subtilis

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P2093

Scholtz JM

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P2860

The high-resolution structure of the histidine-containing phosphocarrier protein HPr from Escherichia coli determined by restrained molecular dynamics from nuclear magnetic resonance nuclear Overhauser effect data

The 2.0-A resolution structure of Escherichia coli histidine-containing phosphocarrier protein HPr. A redetermination

Protein stability curves

Primary structure effects on peptide group hydrogen exchange

Determination and analysis of urea and guanidine hydrochloride denaturation curves

Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants

Stability of protein structure and hydrophobic interaction.

Mechanistic and physiological consequences of HPr(ser) phosphorylation on the activities of the phosphoenolpyruvate:sugar phosphotransferase system in gram-positive bacteria: studies with site-specific mutants of HPr.

The bacterial phosphoenolpyruvate: glycose phosphotransferase system.

Thermodynamics of unfolding for turkey ovomucoid third domain: thermal and chemical denaturation.

P304

35-43

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scholarly article

P356

10.1002/PRO.5560040106

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1

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4

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15426370

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7773175

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2142964

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