Cotranslational structure acquisition of nascent polypeptides monitored by NMR spectroscopy
about
Co- and Post-Translational Protein Folding in the ERA comparison of the folding characteristics of free and ribosome-tethered polypeptide chains using limited proteolysis and mass spectrometryKinetic analysis of ribosome-bound fluorescent proteins reveals an early, stable, cotranslational folding intermediate.Folding of a single domain protein entering the endoplasmic reticulum precedes disulfide formation.Protein folding at the exit tunnel.In vivo translation rates can substantially delay the cotranslational folding of the Escherichia coli cytosolic proteomeHigh yield expression of catalytically active USP18 (UBP43) using a Trigger Factor fusion system.Protein folding in the cell: challenges and progress.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 factorQuantitative determination of ribosome nascent chain stability.Protein folding on the ribosome studied using NMR spectroscopy.The various facets of the protein-folding activity of the ribosome.Accurate prediction of cellular co-translational folding indicates proteins can switch from post- to co-translational foldingThe Exact Nuclear Overhauser Enhancement: Recent Advances.The ribosome in action: Tuning of translational efficiency and protein folding.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.Genetic Code Optimization for Cotranslational Protein Folding: Codon Directional Asymmetry Correlates with Antiparallel Betasheets, tRNA Synthetase ClassesLigand-driven vectorial folding of ribosome-bound human CFTR NBD1Protein 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.Evidence of evolutionary selection for cotranslational folding.Solid-state NMR enhanced by dynamic nuclear polarization as a novel tool for ribosome structural biology
P2860
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P2860
Cotranslational structure acquisition of nascent polypeptides monitored by NMR spectroscopy
description
2010 nî lūn-bûn
@nan
2010 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Cotranslational structure acqu ...... monitored by NMR spectroscopy
@ast
Cotranslational structure acqu ...... monitored by NMR spectroscopy
@en
type
label
Cotranslational structure acqu ...... monitored by NMR spectroscopy
@ast
Cotranslational structure acqu ...... monitored by NMR spectroscopy
@en
prefLabel
Cotranslational structure acqu ...... monitored by NMR spectroscopy
@ast
Cotranslational structure acqu ...... monitored by NMR spectroscopy
@en
P2860
P356
P1476
Cotranslational structure acqu ...... monitored by NMR spectroscopy
@en
P2093
Cédric Eichmann
Roland Riek
P2860
P304
P356
10.1073/PNAS.0914300107
P407
P577
2010-05-03T00:00:00Z