Structure of an intermediate state in protein folding and aggregation
about
Principles and Overview of Sampling Methods for Modeling Macromolecular Structure and DynamicsMechanisms of amyloid formation revealed by solution NMRAccurate Determination of Conformational Transitions in Oligomeric Membrane Proteins.Structures of the Excited States of Phospholamban and Shifts in Their Populations upon PhosphorylationCold denaturation of a protein dimer monitored at atomic resolutionAllosteric inhibition through suppression of transient conformational statesMethionine mutations of outer membrane protein X influence structural stability and beta-barrel unfoldingSH3 domains: modules of protein-protein interactions.Confinement and Stabilization of Fyn SH3 Folding Intermediate Mimetics within the Cavity of the Chaperonin GroEL Demonstrated by Relaxation-Based NMR.Force-dependent switch in protein unfolding pathways and transition-state movements.The energetics of a three-state protein folding system probed by high-pressure relaxation dispersion NMR spectroscopy.Population shuffling between ground and high energy excited states.Intrinsic unfoldase/foldase activity of the chaperonin GroEL directly demonstrated using multinuclear relaxation-based NMR.Fractional enrichment of proteins using [2-(13)C]-glycerol as the carbon source facilitates measurement of excited state 13Cα chemical shifts with improved sensitivity.Electrostatic effects in the folding of the SH3 domain of the c-Src tyrosine kinase: pH-dependence in 3D-domain swapping and amyloid formationMeasuring hydrogen exchange rates in invisible protein excited statesPropensity to form amyloid fibrils is encoded as excitations in the free energy landscape of monomeric proteins.Mapping the structure of amyloid nucleation precursors by protein engineering kinetic analysis.Modulation of the stability of amyloidogenic precursors by anion binding strongly influences the rate of amyloid nucleation.Insights into the folding and unfolding processes of wild-type and mutated SH3 domain by molecular dynamics and replica exchange molecular dynamics simulations.Microcanonical thermostatistics of coarse-grained proteins with amyloidogenic propensity.Site-selective 13C labeling of proteins using erythroseAn off-pathway folding intermediate of an acyl carrier protein domain coexists with the folded and unfolded states under native conditions.ALMOST: an all atom molecular simulation toolkit for protein structure determination.Predicting protein backbone chemical shifts from Cα coordinates: extracting high resolution experimental observables from low resolution models.The quiet renaissance of protein nuclear magnetic resonance.Protein structure prediction using global optimization by basin-hopping with NMR shift restraints.Folding of the four-helix bundle FF domain from a compact on-pathway intermediate state is governed predominantly by water motion.Cyclophilin A catalyzes proline isomerization by an electrostatic handle mechanism.Fast and accurate fitting of relaxation dispersion data using the flexible software package GLOVE.Defining a length scale for millisecond-timescale protein conformational exchange.The non-uniform early structural response of globular proteins to cold denaturing conditions: a case study with Yfh1.Pressure-induced structural transition of mature HIV-1 protease from a combined NMR/MD simulation approach.Signatures of protein thermal denaturation and local hydrophobicity in domain specific hydration behavior: a comparative molecular dynamics study.Measurement of histidine pKa values and tautomer populations in invisible protein states.Chemical exchange in biomacromolecules: past, present, and future.Structural dynamics and conformational equilibria of SERCA regulatory proteins in membranes by solid-state NMR restrained simulations.Self-assembly of the chaperonin GroEL nanocage induced at submicellar detergentQuantifying the Sources of Kinetic Frustration in Folding Simulations of Small Proteins.Visualizing transient dark states by NMR spectroscopy.
P2860
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P2860
Structure of an intermediate state in protein folding and aggregation
description
2012 nî lūn-bûn
@nan
2012 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
name
Structure of an intermediate state in protein folding and aggregation
@ast
Structure of an intermediate state in protein folding and aggregation
@en
Structure of an intermediate state in protein folding and aggregation
@nl
type
label
Structure of an intermediate state in protein folding and aggregation
@ast
Structure of an intermediate state in protein folding and aggregation
@en
Structure of an intermediate state in protein folding and aggregation
@nl
prefLabel
Structure of an intermediate state in protein folding and aggregation
@ast
Structure of an intermediate state in protein folding and aggregation
@en
Structure of an intermediate state in protein folding and aggregation
@nl
P2093
P2860
P50
P3181
P356
P1433
P1476
Structure of an intermediate state in protein folding and aggregation
@en
P2093
Andrea Cavalli
Patrick Walsh
Patrik Lundström
Paul Robustelli
Simon Sharpe
P2860
P3181
P356
10.1126/SCIENCE.1214203
P407
P577
2012-04-20T00:00:00Z