Probing ribosome-nascent chain complexes produced in vivo by NMR spectroscopy.
about
A structural ensemble of a ribosome-nascent chain complex during cotranslational protein folding.Kinetic analysis of ribosome-bound fluorescent proteins reveals an early, stable, cotranslational folding intermediate.Full reconstruction of a vectorial protein folding pathway by atomic force microscopy and molecular dynamics simulations.Mechanically unfolding protein L using a laser-feedback-controlled cantilever.Dynamic fluorescence depolarization: a powerful tool to explore protein folding on the ribosomeProtein folding at the exit tunnel.Recent advances in protein NMR spectroscopy and their implications in protein therapeutics research.Increasing the sensitivity of NMR diffusion measurements by paramagnetic longitudinal relaxation enhancement, with application to ribosome-nascent chain complexesStructural characterization of the interaction of α-synuclein nascent chains with the ribosomal surface and trigger factorProtein folding on the ribosome studied using NMR spectroscopy.The various facets of the protein-folding activity of the ribosome.A Multidisciplinary Approach to High Throughput Nuclear Magnetic Resonance Spectroscopy.Folding of proteins with a flavodoxin-like architecture.The Ribosome Restrains Molten Globule Formation in Stalled Nascent FlavodoxinThe ribosome and its role in protein folding: looking through a magnifying glass.A combinatorial method to enable detailed investigation of protein-protein interactions.Structural studies of the N-terminal fragments of the WW domain: Insights into co-translational folding of a beta-sheet protein.Atomic force microscopy captures folded ribosome bound nascent chains.Ligand-driven vectorial folding of ribosome-bound human CFTR NBD1A Novel Method to Evaluate Ribosomal Performance in Cell-Free Protein Synthesis Systems.Protein folding drives disulfide formation.Using SecM arrest sequence as a tool to isolate ribosome bound polypeptides.Structural and energetic determinants of co-translational folding.A strategy for co-translational folding studies of ribosome-bound nascent chain complexes using NMR spectroscopy.Unraveling co-translational protein folding: Concepts and methods.Protein folding: When ribosomes pick the structure.Kinetic modelling indicates that fast-translating codons can coordinate cotranslational protein folding by avoiding misfolded intermediates.Conformational flexibility within the nascent polypeptide-associated complex enables its interactions with structurally diverse client proteins.Solid-state NMR enhanced by dynamic nuclear polarization as a novel tool for ribosome structural biology
P2860
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P2860
Probing ribosome-nascent chain complexes produced in vivo by NMR spectroscopy.
description
2009 nî lūn-bûn
@nan
2009 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Probing ribosome-nascent chain complexes produced in vivo by NMR spectroscopy.
@ast
Probing ribosome-nascent chain complexes produced in vivo by NMR spectroscopy.
@en
Probing ribosome-nascent chain complexes produced in vivo by NMR spectroscopy.
@nl
type
label
Probing ribosome-nascent chain complexes produced in vivo by NMR spectroscopy.
@ast
Probing ribosome-nascent chain complexes produced in vivo by NMR spectroscopy.
@en
Probing ribosome-nascent chain complexes produced in vivo by NMR spectroscopy.
@nl
prefLabel
Probing ribosome-nascent chain complexes produced in vivo by NMR spectroscopy.
@ast
Probing ribosome-nascent chain complexes produced in vivo by NMR spectroscopy.
@en
Probing ribosome-nascent chain complexes produced in vivo by NMR spectroscopy.
@nl
P2860
P50
P356
P1476
Probing ribosome-nascent chain complexes produced in vivo by NMR spectroscopy.
@en
P2093
John Christodoulou
Lisa D Cabrita
P2860
P304
22239-22244
P356
10.1073/PNAS.0903750106
P407
P577
2009-12-17T00:00:00Z