Folding trajectories of human dihydrofolate reductase inside the GroEL GroES chaperonin cavity and free in solution.
about
Chaperonin chamber accelerates protein folding through passive action of preventing aggregationEngineering and Evolution of Molecular Chaperones and Protein Disaggregases with Enhanced ActivityCoexistence of multiple minor states of fatty acid binding protein and their functional relevanceThe C-terminal tails of the bacterial chaperonin GroEL stimulate protein folding by directly altering the conformation of a substrate proteinAction of the chaperonin GroEL/ES on a non-native substrate observed with single-molecule FRET.The ability to enhance the solubility of its fusion partners is an intrinsic property of maltose-binding protein but their folding is either spontaneous or chaperone-mediatedIdentification of endogenous ligands bound to bacterially expressed human and E. coli dihydrofolate reductase by 2D NMR.Cytosolic chaperones mediate quality control of higher-order septin assembly in budding yeast.Structural determination of biomolecular interfaces by nuclear magnetic resonance of proteins with reduced proton densityDevelopment of free-energy-based models for chaperonin containing TCP-1 mediated folding of actin.Repetitive protein unfolding by the trans ring of the GroEL-GroES chaperonin complex stimulates folding.Effects of interactions with the GroEL cavity on protein folding rates.GroEL/GroES cycling: ATP binds to an open ring before substrate protein favoring protein binding and production of the native state.Chaperones GroEL/GroES accelerate the refolding of a multidomain protein through modulating on-pathway intermediates.The GroEL/GroES cis cavity as a passive anti-aggregation device.Protein dynamics and function from solution state NMR spectroscopy.How do chaperonins fold protein?Single-molecule nanopore enzymology.GroEL Recognizes an Amphipathic Helix and Binds to the Hydrophobic Side.Amino acid-selective segmental isotope labeling of multidomain proteins for structural biology.
P2860
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P2860
Folding trajectories of human dihydrofolate reductase inside the GroEL GroES chaperonin cavity and free in solution.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
2007年论文
@zh
2007年论文
@zh-cn
name
Folding trajectories of human ...... n cavity and free in solution.
@ast
Folding trajectories of human ...... n cavity and free in solution.
@en
type
label
Folding trajectories of human ...... n cavity and free in solution.
@ast
Folding trajectories of human ...... n cavity and free in solution.
@en
prefLabel
Folding trajectories of human ...... n cavity and free in solution.
@ast
Folding trajectories of human ...... n cavity and free in solution.
@en
P2860
P50
P356
P1476
Folding trajectories of human ...... n cavity and free in solution.
@en
P2093
S Walter Englander
Wayne A Fenton
P2860
P304
20788-20792
P356
10.1073/PNAS.0710042105
P407
P577
2007-12-19T00:00:00Z