Structure of an intermediate state in protein folding and aggregation - Wikidata - wikimedia - TriplyDB

Structure of an intermediate state in protein folding and aggregation

Structure of an intermediate state in protein folding and aggregation

http://www.wikidata.org/entity/Q27678629

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Principles and Overview of Sampling Methods for Modeling Macromolecular Structure and Dynamics Mechanisms of amyloid formation revealed by solution NMR Accurate Determination of Conformational Transitions in Oligomeric Membrane Proteins.Structures of the Excited States of Phospholamban and Shifts in Their Populations upon Phosphorylation Cold denaturation of a protein dimer monitored at atomic resolution Allosteric inhibition through suppression of transient conformational states Methionine mutations of outer membrane protein X influence structural stability and beta-barrel unfolding SH3 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 formation Measuring hydrogen exchange rates in invisible protein excited states Propensity 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 erythrose An 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 detergent Quantifying the Sources of Kinetic Frustration in Folding Simulations of Small Proteins.Visualizing transient dark states by NMR spectroscopy.

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Structure of an intermediate state in protein folding and aggregation

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2012年の論文

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Structure of an intermediate state in protein folding and aggregation

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Structure of an intermediate state in protein folding and aggregation

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Structure of an intermediate state in protein folding and aggregation

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Structure of an intermediate state in protein folding and aggregation

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Structure of an intermediate state in protein folding and aggregation

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Structure of an intermediate state in protein folding and aggregation

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Structure of an intermediate state in protein folding and aggregation

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Structure of an intermediate state in protein folding and aggregation

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Structure of an intermediate state in protein folding and aggregation

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Andrea Cavalli

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Patrick Walsh

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Patrik Lundström

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Paul Robustelli

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Simon Sharpe

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P2860

Natural beta-sheet proteins use negative design to avoid edge-to-edge aggregation.

TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts

Crystallographic structure of the SH3 domain of the human c-Yes tyrosine kinase: loop flexibility and amyloid aggregation

Theoretical and experimental demonstration of the importance of specific nonnative interactions in protein folding

Structures of invisible, excited protein states by relaxation dispersion NMR spectroscopy

A transient and low-populated protein-folding intermediate at atomic resolution

Solution structure and ligand-binding site of the SH3 domain of the p85 alpha subunit of phosphatidylinositol 3-kinase

Measurement of J and dipolar couplings from simplified two-dimensional NMR spectra

Protein misfolding, functional amyloid, and human disease

Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide

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362-6

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1811817

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10.1126/SCIENCE.1214203

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6079

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336

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Michele Vendruscolo

Arash Zarrine-Afsar

Philipp Neudecker

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2012-04-20T00:00:00Z

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224770258

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protein structure

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