[ASAP] The Human Fragile X Mental Retardation Protein Inhibits the Elongation Step of Translation through Its RGG and C-Terminal Domains
The Human Fragile X Mental Retardation Protein Inhibits the Elongation Step of Translation through Its RGG and C-Terminal Domains
https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.0c00534/20200929/images/medium/bi0c00534_0006.gif
Biochemistry
DOI: 10.1021/acs.biochem.0c00534
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09-29-2020 07:53 PM
[ASAP] Characterization of Interactions and Phospholipid Transfer between Substrate Binding Proteins of the OmpC-Mla System
Characterization of Interactions and Phospholipid Transfer between Substrate Binding Proteins of the OmpC-Mla System
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00897/20181008/images/medium/bi-2018-00897d_0003.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b00897
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11-25-2018 06:02 AM
Confinement and Stabilization of Fyn SH3 Folding IntermediateMimetics within the Cavity of the Chaperonin GroEL Demonstrated byRelaxation-Based NMR
Confinement and Stabilization of Fyn SH3 Folding IntermediateMimetics within the Cavity of the Chaperonin GroEL Demonstrated byRelaxation-Based NMR
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b01237/20170208/images/medium/bi-2016-01237h_0004.gif
Biochemistry
DOI: 10.1021/acs.biochem.6b01237
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02-09-2017 12:19 PM
[NMR paper] Confinement and stabilization of Fyn SH3 folding interme-diate mimetics within the cavity of the chaperonin GroEL demonstrated by relaxation-based NMR.
Confinement and stabilization of Fyn SH3 folding interme-diate mimetics within the cavity of the chaperonin GroEL demonstrated by relaxation-based NMR.
Related Articles Confinement and stabilization of Fyn SH3 folding interme-diate mimetics within the cavity of the chaperonin GroEL demonstrated by relaxation-based NMR.
Biochemistry. 2017 Feb 03;:
Authors: Libich DS, Tugarinov V, Ghirlando R, Clore GM
Abstract
The interaction of two folding intermediate mimetics of the model protein substrate Fyn SH3 with the chaperonin GroEL, a...
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02-06-2017 11:28 AM
[NMR paper] Probing the transient dark state of substrate binding to GroEL by relaxation-based solution NMR.
Probing the transient dark state of substrate binding to GroEL by relaxation-based solution NMR.
Probing the transient dark state of substrate binding to GroEL by relaxation-based solution NMR.
Proc Natl Acad Sci U S A. 2013 Jun 24;
Authors: Libich DS, Fawzi NL, Ying J, Clore GM
Abstract
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06-27-2013 02:10 PM
NMR spectroscopy with the stringent substrate rhodanese bound to the single-ring variant SR1 of the E. coli chaperonin GroEL.
NMR spectroscopy with the stringent substrate rhodanese bound to the single-ring variant SR1 of the E. coli chaperonin GroEL.
NMR spectroscopy with the stringent substrate rhodanese bound to the single-ring variant SR1 of the E. coli chaperonin GroEL.
Protein Sci. 2011 Jun 1;
Authors: Koculi E, Horst R, Horwich AL, Wüthrich K
NMR observation of the uniformly (2) H,(15) N-labeled stringent 33 kDa substrate protein rhodanese in a productive complex with the uniformly (14) N-labeled 400 kDa single-ring version of the E. coli chaperonin GroEL, SR1,...
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[NMR paper] Direct NMR observation of a substrate protein bound to the chaperonin GroEL.
Direct NMR observation of a substrate protein bound to the chaperonin GroEL.
Related Articles Direct NMR observation of a substrate protein bound to the chaperonin GroEL.
Proc Natl Acad Sci U S A. 2005 Sep 6;102(36):12748-53
Authors: Horst R, Bertelsen EB, Fiaux J, Wider G, Horwich AL, Wüthrich K
The reaction cycle and the major structural states of the molecular chaperone GroEL and its cochaperone, GroES, are well characterized. In contrast, very little is known about the nonnative states of the substrate polypeptide acted on by the...
![[ASAP] Retardation of Folding Rates of Substrate Proteins in the Nanocage of GroEL](http://www.bionmr.com/forum/iconimages/journal-club-9/%5Basap%5D-retardation-folding-rates-substrate-proteins-nanocage-groel_ltr.gif)
[ASAP] Retardation of Folding Rates of Substrate Proteins in the Nanocage of GroEL
Linear Mode
