Conformational specificity of the chaperonin GroEL for the compact folding intermediates of alpha-lactalbumin.
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Significant hydrogen exchange protection in GroEL-bound DHFR is maintained during iterative rounds of substrate cyclingA structural model for GroEL-polypeptide recognitionInteraction of p53 with the CCT complex promotes protein folding and wild-type p53 activityChaperoninsInteraction of GroEL with a highly structured folding intermediate: iterative binding cycles do not involve unfolding.FK506-Binding protein 22 from a psychrophilic bacterium, a cold shock-inducible peptidyl prolyl isomerase with the ability to assist in protein folding.Functional Subunits of Eukaryotic Chaperonin CCT/TRiC in Protein Folding.A zinc finger-like domain of the molecular chaperone DnaJ is involved in binding to denatured protein substrates.Mechanism of chaperonin action: GroES binding and release can drive GroEL-mediated protein folding in the absence of ATP hydrolysis.Limited proteolysis of bovine alpha-lactalbumin: isolation and characterization of protein domains.Asymmetry of the GroEL-GroES complex under physiological conditions as revealed by small-angle x-ray scattering.GroEL-mediated protein folding: making the impossible, possible.beta-Lactamase binds to GroEL in a conformation highly protected against hydrogen/deuterium exchange.GroEL-assisted protein folding: does it occur within the chaperonin inner cavity?The N-terminal region of the luteovirus readthrough domain determines virus binding to Buchnera GroEL and is essential for virus persistence in the aphidGroEL binds a late folding intermediate of phage P22 coat protein.In vivo newly translated polypeptides are sequestered in a protected folding environment.GroEL-mediated protein folding.Analysis of peptides and proteins in their binding to GroEL.The chaperonin cycle cannot substitute for prolyl isomerase activity, but GroEL alone promotes productive folding of a cyclophilin-sensitive substrate to a cyclophilin-resistant formPeptide and protein binding in the axial channel of Hsp104. Insights into the mechanism of protein unfoldingFactors governing the substrate recognition by GroEL chaperone: a sequence correlation approach.GroEL Recognizes an Amphipathic Helix and Binds to the Hydrophobic Side.Evidence for a conformational change in a class II major histocompatibility complex molecule occurring in the same pH range where antigen binding is enhanced.Cooperation of enzymatic and chaperone functions of trigger factor in the catalysis of protein foldingThe molecular chaperone alpha-crystallin is in kinetic competition with aggregation to stabilize a monomeric molten-globule form of alpha-lactalbumin.
P2860
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P2860
Conformational specificity of the chaperonin GroEL for the compact folding intermediates of alpha-lactalbumin.
description
1994 nî lūn-bûn
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1994年の論文
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1994年学术文章
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name
Conformational specificity of ...... mediates of alpha-lactalbumin.
@en
type
label
Conformational specificity of ...... mediates of alpha-lactalbumin.
@en
prefLabel
Conformational specificity of ...... mediates of alpha-lactalbumin.
@en
P2093
P2860
P1433
P1476
Conformational specificity of ...... mediates of alpha-lactalbumin.
@en
P2093
J J Ewbank
M K Hayer-Hartl
T E Creighton
P2860
P304
P407
P577
1994-07-01T00:00:00Z