BeF(x) stops the chaperonin cycle of GroEL-GroES and generates a complex with double folding chambers.
about
Dynamic Complexes in the Chaperonin-Mediated Protein Folding CycleChaperonin GroEL uses asymmetric and symmetric reaction cycles in response to the concentration of non-native substrate proteinsProbing the functional mechanism of Escherichia coli GroEL using circular permutation.Action of the chaperonin GroEL/ES on a non-native substrate observed with single-molecule FRET.Formation and structures of GroEL:GroES2 chaperonin footballs, the protein-folding functional formProbing the sequence of conformationally induced polarity changes in the molecular chaperonin GroEL with fluorescence spectroscopy.Football- and bullet-shaped GroEL-GroES complexes coexist during the reaction cycle.Asymmetry of the GroEL-GroES complex under physiological conditions as revealed by small-angle x-ray scattering.A gradient of ATP affinities generates an asymmetric power stroke driving the chaperonin TRIC/CCT folding cycle.ATP ground- and transition states of bacterial enhancer binding AAA+ ATPases support complex formation with their target protein, sigma54.Conformational shift in the closed state of GroEL induced by ATP-binding triggers a transition to the open state.Substrate protein switches GroE chaperonins from asymmetric to symmetric cycling by catalyzing nucleotide exchange.Symmetric GroEL:GroES2 complexes are the protein-folding functional form of the chaperonin nanomachineRevisiting the GroEL-GroES reaction cycle via the symmetric intermediate implied by novel aspects of the GroEL(D398A) mutant.Single-molecule study on the decay process of the football-shaped GroEL-GroES complex using zero-mode waveguides.Probing open conformation of GroEL rings by cross-linking reveals single and double open ring structures of GroEL in ADP and ATP.Single-molecule observation of protein folding in symmetric GroEL-(GroES)2 complexes.Effects of C-terminal Truncation of Chaperonin GroEL on the Yield of In-cage Folding of the Green Fluorescent Protein.Asp-52 in combination with Asp-398 plays a critical role in ATP hydrolysis of chaperonin GroEL.Denatured proteins facilitate the formation of the football-shaped GroEL-(GroES)2 complex.Characterization of archaeal group II chaperonin-ADP-metal fluoride complexes: implications that group II chaperonins operate as a "two-stroke engine".Leu309 plays a critical role in the encapsulation of substrate protein into the internal cavity of GroEL.Hydrophilic residues 526 KNDAAD 531 in the flexible C-terminal region of the chaperonin GroEL are critical for substrate protein folding within the central cavity.Disassembly/reassembly strategy for the production of highly pure GroEL, a tetradecameric supramolecular machine, suitable for quantitative NMR, EPR and mutational studies.Chaperonin GroEL accelerates protofibril formation and decorates fibrils of the Het-s prion protein.Physicochemical Properties of the Mammalian Molecular Chaperone HSP60.
P2860
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P2860
BeF(x) stops the chaperonin cycle of GroEL-GroES and generates a complex with double folding chambers.
description
2004 nî lūn-bûn
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2004年の論文
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2004年学术文章
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2004年学术文章
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2004年学术文章
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name
BeF
@nl
BeF(x) stops the chaperonin cy ...... with double folding chambers.
@en
type
label
BeF
@nl
BeF(x) stops the chaperonin cy ...... with double folding chambers.
@en
prefLabel
BeF
@nl
BeF(x) stops the chaperonin cy ...... with double folding chambers.
@en
P2093
P2860
P356
P1476
BeF(x) stops the chaperonin cy ...... x with double folding chambers
@en
P2093
Ayumi Koike-Takeshita
Keigo Tsukuda
Masasuke Yoshida
P2860
P304
45737-45743
P356
10.1074/JBC.M406795200
P407
P577
2004-08-30T00:00:00Z