Phosphorylation-induced torsion-angle strain in the active center of HPr, detected by NMR and restrained molecular dynamics refinement.

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Phosphorylation on histidine is accompanied by localized structural changes in the phosphocarrier protein, HPr from Bacillus subtilis.An extended sampling of the configurational space of HPr from E. coli.

P2860

Q41914232-57968500-2F2B-4142-B773-6BC447BDDF40 Q54577829-51BF383A-98C7-40C2-999D-2A5B169FAD42

P2860

Phosphorylation-induced torsion-angle strain in the active center of HPr, detected by NMR and restrained molecular dynamics refinement.

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http://www.wikidata.org/entity/Q36826845

description

1996 nî lūn-bûn

@nan

1996年の論文

@ja

1996年論文

@yue

1996年論文

@zh-hant

1996年論文

@zh-hk

1996年論文

@zh-mo

1996年論文

@zh-tw

1996年论文

@wuu

1996年论文

@zh

1996年论文

@zh-cn

name

Phosphorylation-induced torsio ...... molecular dynamics refinement.

@en

type

Item

label

Phosphorylation-induced torsio ...... molecular dynamics refinement.

@en

prefLabel

Phosphorylation-induced torsio ...... molecular dynamics refinement.

@en

P1476

Phosphorylation-induced torsio ...... molecular dynamics refinement.

@en

P2093

De Groot BL

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Robillard GT

http://www.w3.org/2001/XMLSchema#string

Scheek RM

http://www.w3.org/2001/XMLSchema#string

Van Der Spoel D

http://www.w3.org/2001/XMLSchema#string

Van Nuland NA

http://www.w3.org/2001/XMLSchema#string

Wiersma JA

http://www.w3.org/2001/XMLSchema#string

P2860

Phosphoenolpyruvate:carbohydrate phosphotransferase systems of bacteria

Refined structures of the active Ser83-->Cys and impaired Ser46-->Asp histidine-containing phosphocarrier proteins

The 1.6 A structure of histidine-containing phosphotransfer protein HPr from Streptococcus faecalis

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

Sequence analyses and evolutionary relationships among the energy-coupling proteins Enzyme I and HPr of the bacterial phosphoenolpyruvate: sugar phosphotransferase system.

The solution structure of the histidine-containing protein (HPr) from Staphylococcus aureus as determined by two-dimensional 1H-NMR spectroscopy.

Structure of the histidine-containing phosphocarrier protein HPr from Bacillus subtilis at 2.0-A resolution

The effects of phosphorylation on the structure and function of proteins.

Solution structure of the phosphocarrier protein HPr from Bacillus subtilis by two-dimensional NMR spectroscopy.

P304

442-446

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P31

scholarly article

P356

10.1002/PRO.5560050305

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http://www.w3.org/2001/XMLSchema#string

P478

http://www.w3.org/2001/XMLSchema#string

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1996-03-01T00:00:00Z

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P5875

43432346

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P698

8868480

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P921

phosphorylation

P932

2143356

http://www.w3.org/2001/XMLSchema#string

Phosphorylation-induced torsion-angle strain in the active center of HPr, detected by NMR and restrained molecular dynamics refinement.

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P2860

P2860

Phosphorylation-induced torsion-angle strain in the active center of HPr, detected by NMR and restrained molecular dynamics refinement.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P5875

P698

P921

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P5875

P698

P921

P932