Setting the chaperonin timer: the effects of K+ and substrate protein on ATP hydrolysis.
about
Use of thallium to identify monovalent cation binding sites in GroELCrystal structure of a GroEL-ADP complex in the relaxed allosteric state at 2.7 A resolutionChaperonin GroEL uses asymmetric and symmetric reaction cycles in response to the concentration of non-native substrate proteinsUsing ¹⁵N-ammonium to characterise and map potassium binding sites in proteins by NMR spectroscopy.Out-of-equilibrium conformational cycling of GroEL under saturating ATP concentrationsGroEL actively stimulates folding of the endogenous substrate protein PepQFormation and structures of GroEL:GroES2 chaperonin footballs, the protein-folding functional formIdentification of elements that dictate the specificity of mitochondrial Hsp60 for its co-chaperonin.Nucleotide-induced conformational changes of tetradecameric GroEL mapped by H/D exchange monitored by FT-ICR mass spectrometrySetting the chaperonin timer: a two-stroke, two-speed, protein machine.Measuring how much work the chaperone GroEL can do.Putting handcuffs on the chaperonin GroEL.Repetitive protein unfolding by the trans ring of the GroEL-GroES chaperonin complex stimulates folding.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 nanomachineSingle-molecule observation of protein folding in symmetric GroEL-(GroES)2 complexes.Denatured proteins facilitate the formation of the football-shaped GroEL-(GroES)2 complex.Disassembly/reassembly strategy for the production of highly pure GroEL, a tetradecameric supramolecular machine, suitable for quantitative NMR, EPR and mutational studies.Folding of maltose binding protein outside of and in GroEL.Chaperonin GroEL accelerates protofibril formation and decorates fibrils of the Het-s prion protein.
P2860
Q27657923-82EFE9E9-5AB7-48A7-B406-3C1ED3C25B31Q27679114-17C6C765-B472-4E87-B7BD-D36EED1ABDA0Q28074574-3D713595-6770-40B9-B4D4-703A85B46778Q33593580-704C9D61-C22E-44D7-A654-32B5D27CEFECQ33778946-800F2446-C434-48C3-9EC0-AC2FC02FDD76Q33871444-947B402E-4FA7-4EE9-885A-4DA4DC064556Q34144755-5DBF5E70-9D76-4636-B004-A0CC211BCB6BQ34506502-62282C50-75C4-4A1F-A96B-1D663B97F171Q36605501-C5ACC917-912B-4A78-BB27-4C1804AF6635Q36967128-86AAB988-CC2A-4A07-8885-AAA0B542E570Q36990800-762B636B-A2DB-444C-9AA6-338A3C09D9FBQ36991003-5F7913F1-3A59-4675-AC4C-DF4278C4CA3EQ37312135-A77812DD-707B-49C5-AED4-209BF442A0C3Q37319595-FD956F1D-B2E4-48E4-A94A-936CB18FB8A9Q37319749-EB074A91-43C4-4784-B8F2-7A00942894F7Q42118511-742F8483-B503-4291-B977-1EC253D60381Q43178484-3338EB79-F9B3-4462-B400-EC133534E527Q47185650-6DA8C76D-30AA-45BA-83FD-94CD774BBDA1Q47236838-6E5E66E7-1D7F-4A7A-A6A0-20244E6A4CB6Q47981671-F5AA99FC-FBD8-40D5-9CDB-D64FDB94B82E
P2860
Setting the chaperonin timer: the effects of K+ and substrate protein on ATP hydrolysis.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
Setting the chaperonin timer: the effects of K+ and substrate protein on ATP hydrolysis.
@en
type
label
Setting the chaperonin timer: the effects of K+ and substrate protein on ATP hydrolysis.
@en
prefLabel
Setting the chaperonin timer: the effects of K+ and substrate protein on ATP hydrolysis.
@en
P2093
P2860
P356
P1476
Setting the chaperonin timer: the effects of K+ and substrate protein on ATP hydrolysis.
@en
P2093
George H Lorimer
Jennifer S Gresham
John P Grason
Lusiana Widjaja
Sarah C Wehri
P2860
P304
17334-17338
P356
10.1073/PNAS.0807429105
P407
P577
2008-11-06T00:00:00Z