HdeB chaperone activity is coupled to its intrinsic dynamic properties.

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Stress-Activated Chaperones: A First Line of Defense.In vivo chloride concentrations surge to proteotoxic levels during acid stress

P2860

Q47821726-F1C8701E-5097-4994-9CD1-5D4A05EE220B Q57452400-CE13EDC4-082E-40F5-B50C-A8FA9863A4EA

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HdeB chaperone activity is coupled to its intrinsic dynamic properties.

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http://www.wikidata.org/entity/Q36305554

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2015 nî lūn-bûn

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2015年学术文章

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HdeB chaperone activity is coupled to its intrinsic dynamic properties.

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HdeB chaperone activity is coupled to its intrinsic dynamic properties.

@en

type

Item

label

HdeB chaperone activity is coupled to its intrinsic dynamic properties.

@ast

HdeB chaperone activity is coupled to its intrinsic dynamic properties.

@en

prefLabel

HdeB chaperone activity is coupled to its intrinsic dynamic properties.

@ast

HdeB chaperone activity is coupled to its intrinsic dynamic properties.

@en

P1476

HdeB chaperone activity is coupled to its intrinsic dynamic properties.

@en

P2093

Chengfeng Yang

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

Jienv Ding

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

Xiaogang Niu

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

Yunfei Hu

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

P2860

HDEA, a periplasmic protein that supports acid resistance in pathogenic enteric bacteria

Recognition dynamics up to microseconds revealed from an RDC-derived ubiquitin ensemble in solution

Salt Bridges Regulate Both Dimer Formation and Monomeric Flexibility in HdeB and May Have a Role in Periplasmic Chaperone Function

ATP-Triggered Conformational Changes Delineate Substrate-Binding and -Folding Mechanics of the GroEL Chaperonin

Integrated description of protein dynamics from room-temperature X-ray crystallography and NMR

Structural Basis for Protein Antiaggregation Activity of the Trigger Factor Chaperone

Crystal structure of Escherichia coli HdeA

Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation

Using NMRView to visualize and analyze the NMR spectra of macromolecules

Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA

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srep16856

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16856

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scholarly article

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10.1038/SREP16856

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English

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

P50

Changwen Jin

P577

2015-11-23T00:00:00Z

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

P5875

284559813

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26593705

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P921

molecular chaperones

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4655364

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

HdeB chaperone activity is coupled to its intrinsic dynamic properties.

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P2860

P2860

HdeB chaperone activity is coupled to its intrinsic dynamic properties.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P407

P478

P50

P577

P5875

P698

P921

P932

P356

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P407

P478

P50

P577

P5875

P698

P921

P932