Repetitive protein unfolding by the trans ring of the GroEL-GroES chaperonin complex stimulates folding.
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GroEL actively stimulates folding of the endogenous substrate protein PepQThe C-terminal tails of the bacterial chaperonin GroEL stimulate protein folding by directly altering the conformation of a substrate proteinDifferential protein expression in Phalaenopsis under low temperature.Folding of newly translated membrane protein CCR5 is assisted by the chaperonin GroEL-GroES.Symmetric GroEL:GroES2 complexes are the protein-folding functional form of the chaperonin nanomachineHow do chaperonins fold protein?The chaperone toolbox at the single-molecule level: From clamping to confining.Molecular chaperones maximize the native state yield on biological times by driving substrates out of equilibrium.Temperature-Dependent Nanomechanics and Topography of Bacteriophage T7
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Repetitive protein unfolding by the trans ring of the GroEL-GroES chaperonin complex stimulates folding.
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article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 10 September 2013
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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name
Repetitive protein unfolding b ...... in complex stimulates folding.
@en
Repetitive protein unfolding b ...... in complex stimulates folding.
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type
label
Repetitive protein unfolding b ...... in complex stimulates folding.
@en
Repetitive protein unfolding b ...... in complex stimulates folding.
@nl
prefLabel
Repetitive protein unfolding b ...... in complex stimulates folding.
@en
Repetitive protein unfolding b ...... in complex stimulates folding.
@nl
P2093
P2860
P356
P1476
Repetitive protein unfolding b ...... in complex stimulates folding.
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P2093
Daniel Shoup
Hays S Rye
Jason Puchalla
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P304
30944-30955
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10.1074/JBC.M113.480178
P407
P577
2013-09-10T00:00:00Z