Solution structures of GroEL and its complex with rhodanese from small-angle neutron scattering.
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Significant hydrogen exchange protection in GroEL-bound DHFR is maintained during iterative rounds of substrate cyclingThe Bacillus subtilis RNase P holoenzyme contains two RNase P RNA and two RNase P protein subunits.Materials Research With Neutrons at NIST.Chaperonins GroEL and GroES: views from atomic force microscopy.Multi-scale simulations provide supporting evidence for the hypothesis of intramolecular protein translocation in GroEL/GroES complexes.Direct NMR observation of a substrate protein bound to the chaperonin GroEL.Monte Carlo modeling of small-angle scattering data from non-interacting homogeneous and heterogeneous particles in solution.Surfactant copolymers prevent aggregation of heat denatured lysozyme.Topologies of a substrate protein bound to the chaperonin GroELAsymmetry of the GroEL-GroES complex under physiological conditions as revealed by small-angle x-ray scattering.GroEL-mediated protein folding: making the impossible, possible.Denaturation and reassembly of chaperonin GroEL studied by solution X-ray scatteringLight-activated DNA binding in a designed allosteric protein.Increased light intensity induces heat shock protein Hsp60 in coral species.GroEL-assisted protein folding: does it occur within the chaperonin inner cavity?Substrate polypeptide presents a load on the apical domains of the chaperonin GroEL.ATP-driven molecular chaperone machines.Effect of the C-terminal truncation on the functional cycle of chaperonin GroEL: implication that the C-terminal region facilitates the transition from the folding-arrested to the folding-competent state.GroEL-mediated protein folding.Analysis of peptides and proteins in their binding to GroEL.Translocation boost protein-folding efficiency of double-barreled chaperonins.GroEL Recognizes an Amphipathic Helix and Binds to the Hydrophobic Side.Triggering protein folding within the GroEL-GroES complex.Effects of C-terminal Truncation of Chaperonin GroEL on the Yield of In-cage Folding of the Green Fluorescent Protein.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.
P2860
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P2860
Solution structures of GroEL and its complex with rhodanese from small-angle neutron scattering.
description
1996 nî lūn-bûn
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1996年の論文
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1996年学术文章
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1996年学术文章
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1996年学术文章
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1996年学术文章
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1996年学术文章
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1996年學術文章
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name
Solution structures of GroEL a ...... mall-angle neutron scattering.
@en
Solution structures of GroEL a ...... mall-angle neutron scattering.
@nl
type
label
Solution structures of GroEL a ...... mall-angle neutron scattering.
@en
Solution structures of GroEL a ...... mall-angle neutron scattering.
@nl
prefLabel
Solution structures of GroEL a ...... mall-angle neutron scattering.
@en
Solution structures of GroEL a ...... mall-angle neutron scattering.
@nl
P2093
P1433
P1476
Solution structures of GroEL a ...... mall-angle neutron scattering.
@en
P2093
Henderson SJ
Joachimiak A
Thiyagarajan P
P356
10.1016/S0969-2126(96)00011-1
P577
1996-01-01T00:00:00Z