About: Protein substrate binding induces conformational changes in the chaperonin GroEL. A suggested mechanism for unfoldase activity

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About: Protein substrate binding induces conformational changes in the chaperonin GroEL. A suggested mechanism for unfoldase activity Goto Sponge Distinct Permalink

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scientific article published on 01 July 2000

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rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в липні 2000 (uk) article scientifique publié en 2000 (fr) im Juli 2000 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu en xunetu de 2000 (ast) scientific article published on 01 July 2000 (en)
publication date	wds:Q73794091-E96A58E1-543A-4F67-952C-41AC59761982
publication date	2000-07-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q73794091-D2712188-6CDF-4E90-9ADD-C37F283830DC
language of work or name	English
cites work	wds:Q73794091-02743BA7-AA96-46CC-AE7B-F01F6F3EAFD3 wds:Q73794091-02D0B701-15FB-42A5-B57E-F94AA1F3AD68 wds:Q73794091-06DA3796-0392-4549-B313-2295EE19ECD7 wds:Q73794091-0C0BD2A9-CAD7-4E6B-ACC3-57BF098C89F9 wds:Q73794091-2491E5C5-8B2A-4784-A199-0F62B1FB8A93 wds:Q73794091-266FD9D6-5FEA-4708-BBA8-0D52A1CF78C6 wds:Q73794091-300510F2-C7F7-429F-8359-3D926F489FD0 wds:Q73794091-322AEBF8-E6F3-4D2F-9DB6-124B33E3450A wds:Q73794091-3C821976-A02C-41D7-BF8D-C7DA34C4B447 wds:Q73794091-4035E352-4BE9-428B-B25A-5509A315A31F wds:Q73794091-508E86C2-5D2A-44DB-B14B-F02ED3B18BFB wds:Q73794091-527BF24D-1382-427B-84FD-7C17362DF280 wds:Q73794091-55EDAB5C-DD0C-45FF-916F-BBE416C602BB wds:Q73794091-64D0BDAE-7B98-488C-8EDA-F30FA8749277 wds:Q73794091-6D6FD2E8-5E5E-4BC2-B403-FB7308AE8081 wds:Q73794091-6DAA7315-BD53-4A55-BF97-2F417A66B144 wds:Q73794091-7945CBED-815A-44E3-A729-168F33D39A57 wds:Q73794091-7D092ED3-23B5-4C03-A2FF-CA7D19B74AD6 wds:Q73794091-7FC9C1E9-CF83-483E-A6B2-1439E8A9BE38 wds:Q73794091-939A5542-EF86-4E73-804E-B43875B760F1 wds:Q73794091-A1C81320-5394-421D-B6ED-818D117ABAD0 wds:Q73794091-AEA1153C-067D-4860-B444-8E8779596DBF wds:Q73794091-B6CF6171-0A55-4855-83EA-520113C4975D wds:Q73794091-B6EF50CE-8FC6-4277-9C33-8A4953C522A9 wds:Q73794091-B7ED2CCD-75E8-463E-BFF0-A61FCC3C353F wds:Q73794091-C9DEB509-9EB1-41DD-A598-FCF57E87B162 wds:Q73794091-CD93C3D7-C1ED-41B1-95E8-7A47941EC571 wds:Q73794091-D61CC798-D3FD-4C91-AD8A-37588D786EBE wds:Q73794091-D78D9EFE-8EEE-47D3-8226-CB3FABCDDE31 wds:Q73794091-D85F8ED7-B708-42D2-9D63-035BE179133E wds:Q73794091-DCB8A74E-B1BD-46C7-97D0-0B706921E62F wds:Q73794091-E0889C31-E5CF-4A83-B6B6-4BFA1F0CEDD7 wds:Q73794091-EEF250F7-7C17-42BF-A5BE-38C3F596498F wds:Q73794091-FCAD668F-1763-418A-9C38-25C85E3402F6
cites work	The kinetics of formation of native ribonuclease during oxidation of the reduced polypeptide chain The molecular chaperonin cpn60 displays local flexibility that is reduced after binding with an unfolded protein Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy. Principles that govern the folding of protein chains The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex Catalysis of amide proton exchange by the molecular chaperones GroEL and SecB Conformational states bound by the molecular chaperones GroEL and secB: a hidden unfolding (annealing) activity The crystal structure of the bacterial chaperonin GroEL at 2.8 A Chaperonin-facilitated protein folding: optimization of rate and yield by an iterative annealing mechanism Mapping the folding intermediate of human carbonic anhydrase II. Probing substructure by chemical reactivity and spin and fluorescence labeling of engineered cysteine residues Destabilization of the complete protein secondary structure on binding to the chaperone GroEL. Characterization of folding intermediates of human carbonic anhydrase II: probing substructure by chemical labeling of SH groups introduced by site-directed mutagenesis A thermodynamic coupling mechanism for GroEL-mediated unfolding Fluorescence-polarization spectrum and electronic-energy transfer in tyrosine, tryptophan and related compounds The crystal structure of a GroEL/peptide complex: plasticity as a basis for substrate diversity Conformational variability in the refined structure of the chaperonin GroEL at 2.8 A resolution Folding around the C-terminus of human carbonic anhydrase II. Kinetic characterization by use of a chemically reactive SH-group introduced by protein engineering EPR mapping of interactions between spin-labeled variants of human carbonic anhydrase II and GroEL: evidence for increased flexibility of the hydrophobic core by the interaction GroEL-GroES cycling: ATP and nonnative polypeptide direct alternation of folding-active rings Chaperonin function: folding by forced unfolding Failure of Energy Transfer between Identical Aromatic Molecules on Excitation at the Long Wave Edge of the Absorption Spectrum Segmental dynamics of the cytoplasmic domain of erythrocyte band 3 determined by time-resolved fluorescence anisotropy: sensitivity to pH and ligand binding Nature and consequences of GroEL-protein interactions. Properties of spin and fluorescent labels at a receptor-ligand interface Chaperone-percolator model: a possible molecular mechanism of Anfinsen-cage-type chaperones Stability of the asymmetric Escherichia coli chaperonin complex. Guanidine chloride causes rapid dissociation GroEL provides a folding pathway with lower apparent activation energy compared to spontaneous refolding of human carbonic anhydrase II. GroEL reversibly binds to, and causes rapid inactivation of, human carbonic anhydrase II at high temperatures GroEL/ES-mediated refolding of human carbonic anhydrase II: role of N-terminal helices as recognition motifs for GroEL Rotational and conformational dynamics of Escherichia coli ribosomal protein L7/L12 Ligand-induced conformational changes of GroEL are dependent on the bound substrate polypeptide Conformational changes at the nucleotide binding of GroEL induced by binding of protein substrates. Luminescence studies Nucleotide and Mg2+ induced conformational changes in GroEL can be detected by sulfhydryl labeling Interaction of 4,4'-dithiodipyridine with Cys(458) triggers disassembly of GroEL
author name string	wds:Q73794091-4587D4A5-69F5-49FD-99FA-A47B6A0E202F wds:Q73794091-669B6135-F857-45F7-A4F9-79DE57899BCB wds:Q73794091-845269FC-0E6B-4C77-A011-F7BC2AC2BC73 wds:Q73794091-DE46F1E3-C41B-4C02-8CBD-DDA93BC2A10B wds:Q73794091-EF179E65-62EF-41A5-BD35-7A0EBB329071
author name string	Persson M Carlsson U Hammarström P Lindgren M Owenius R
rdfs:label	Protein substrate binding induces conformational changes in the chaperonin GroEL. A suggested mechanism for unfoldase activity (en) Protein substrate binding induces conformational changes in the chaperonin GroEL. A suggested mechanism for unfoldase activity (nl)
skos:prefLabel	Protein substrate binding induces conformational changes in the chaperonin GroEL. A suggested mechanism for unfoldase activity (en) Protein substrate binding induces conformational changes in the chaperonin GroEL. A suggested mechanism for unfoldase activity (nl)
name	Protein substrate binding induces conformational changes in the chaperonin GroEL. A suggested mechanism for unfoldase activity (en) Protein substrate binding induces conformational changes in the chaperonin GroEL. A suggested mechanism for unfoldase activity (nl)
title	wds:Q73794091-E0D75D11-F199-4021-B835-E0B8C39147A8
title	Protein substrate binding induces conformational changes in the chaperonin GroEL. A suggested mechanism for unfoldase activity (en)
page(s)	wds:Q73794091-925214A9-EC84-4A81-9267-220EDD2B5BAE
page(s)	22832-22838
instance of	wds:Q73794091-F20225EE-C50A-429F-8C28-CF7AD4F1E4DA

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