Measurement of protein unfolding/refolding kinetics and structural characterization of hidden intermediates by NMR relaxation dispersion.
about
Characterization of protein unfolding with solid-state nanoporesStructural Instability Tuning as a Regulatory Mechanism in Protein-Protein InteractionsCold denaturation of a protein dimer monitored at atomic resolutionVisualizing the formation of an RNA folding intermediate through a fast highly modular secondary structure switchMapping molecular flexibility of proteins with site-directed spin labeling: a case study of myoglobin.Fast and accurate fitting of relaxation dispersion data using the flexible software package GLOVE.Mapping protein conformational heterogeneity under pressure with site-directed spin labeling and double electron-electron resonance.Measurement of histidine pKa values and tautomer populations in invisible protein states.Chemical exchange in biomacromolecules: past, present, and future.Probing the non-native H helix translocation in apomyoglobin folding intermediates.Evidence for close side-chain packing in an early protein folding intermediate previously assumed to be a molten globule.1-Anilino-8-naphthalene sulfonate (ANS) is not a desirable probe for determining the molten globule state of chymopapainGuanidine-HCl dependent structural unfolding of M-crystallin: fluctuating native state like topologies and intermolecular association.The maturational refolding of the β-hairpin motif of equine infectious anemia virus capsid protein extends its helix α1 at capsid assembly locus.Multi-probe relaxation dispersion measurements increase sensitivity to protein dynamics.Visualizing transient low-populated structures of RNA.Conformational selection and adaptation to ligand binding in T4 lysozyme cavity mutants.Circular dichroism and site-directed spin labeling reveal structural and dynamical features of high-pressure states of myoglobin.Protein dynamics and function from solution state NMR spectroscopy.Practical considerations for investigation of protein conformational dynamics by 15N R 1ρ relaxation dispersion.Folding of apomyoglobin: Analysis of transient intermediate structure during refolding using quick hydrogen deuterium exchange and NMR.Extracting protein dynamics information from overlapped NMR signals using relaxation dispersion difference NMR spectroscopy.Understanding the mechanism of prosegment-catalyzed folding by solution NMR spectroscopy.A simple three-dimensional-focusing, continuous-flow mixer for the study of fast protein dynamics.Allosteric activation of the Par-6 PDZ via a partial unfolding transition.How Does Your Protein Fold? Elucidating the Apomyoglobin Folding Pathway.Nanopore Sensing of Protein Folding.Thermal unfolding of myoglobin in the Landau-Ginzburg-Wilson approach.Molecular dynamics ensemble refinement of the heterogeneous native state of NCBD using chemical shifts and NOEs
P2860
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P2860
Measurement of protein unfolding/refolding kinetics and structural characterization of hidden intermediates by NMR relaxation dispersion.
description
2011 nî lūn-bûn
@nan
2011 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Measurement of protein unfoldi ...... by NMR relaxation dispersion.
@ast
Measurement of protein unfoldi ...... by NMR relaxation dispersion.
@en
type
label
Measurement of protein unfoldi ...... by NMR relaxation dispersion.
@ast
Measurement of protein unfoldi ...... by NMR relaxation dispersion.
@en
prefLabel
Measurement of protein unfoldi ...... by NMR relaxation dispersion.
@ast
Measurement of protein unfoldi ...... by NMR relaxation dispersion.
@en
P2860
P356
P1476
Measurement of protein unfoldi ...... by NMR relaxation dispersion.
@en
P2093
Derrick W Meinhold
P2860
P304
P356
10.1073/PNAS.1105682108
P407
P50
P577
2011-05-11T00:00:00Z