Temperature-dependent solvation modulates the dimensions of disordered proteins.
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Insights into Coupled Folding and Binding Mechanisms from Kinetic StudiesShedding light on protein folding, structural and functional dynamics by single molecule studiesRelating sequence encoded information to form and function of intrinsically disordered proteinsTowards a structural biology of the hydrophobic effect in protein foldingEffects of Mutations on the Reconfiguration Rate of α-SynucleinThe hydrophobic temperature dependence of amino acids directly calculated from protein structuresSolubility and aggregation of Gly(5) in water.A coarse-grained model for polyglutamine aggregation modulated by amphipathic flanking sequencesBalanced Protein-Water Interactions Improve Properties of Disordered Proteins and Non-Specific Protein AssociationAlanine and proline content modulate global sensitivity to discrete perturbations in disordered proteins.Free energetics of carbon nanotube association in aqueous inorganic NaI salt solutions: Temperature effects using all-atom molecular dynamics simulations.Quantitative interpretation of FRET experiments via molecular simulation: force field and validation.Targeting intrinsically disordered proteins in rational drug discovery.Hydrodynamic Radii of Intrinsically Disordered Proteins Determined from Experimental Polyproline II Propensities.Thermodynamics of protein destabilization in live cellsThe inverted free energy landscape of an intrinsically disordered peptide by simulations and experiments.Conformational dynamics and self-association of intrinsically disordered Huntingtin exon 1 in cells.Comprehensive structural and dynamical view of an unfolded protein from the combination of single-molecule FRET, NMR, and SAXS.Consistent View of Polypeptide Chain Expansion in Chemical Denaturants from Multiple Experimental Methods.Dimension conversion and scaling of disordered protein chains.Empirical Optimization of Interactions between Proteins and Chemical Denaturants in Molecular Simulations.The Proline/Glycine-Rich Region of the Biofilm Adhesion Protein Aap Forms an Extended Stalk that Resists Compaction.Slow Internal Dynamics and Charge Expansion in the Disordered Protein CGRP: A Comparison with Amylin.Probing the Action of Chemical Denaturant on an Intrinsically Disordered Protein by Simulation and Experiment.Integrated view of internal friction in unfolded proteins from single-molecule FRET, contact quenching, theory, and simulations.Exploring the Denatured State Ensemble by Single-Molecule Chemo-Mechanical Unfolding: The Effect of Force, Temperature, and Urea.Single-molecule fluorescence-based analysis of protein conformation, interaction, and oligomerization in cellular systems.Comment on "Thermal compaction of the intrinsically disordered protein tau: entropic, structural, and hydrophobic factors" by A. Battisti, G. Ciasca, A. Grottesi and A. Tenenbaum, Phys. Chem. Chem. Phys., 2017, 19, 8435.Combining short- and long-range fluorescence reporters with simulations to explore the intramolecular dynamics of an intrinsically disordered protein.Structural properties of amyloid β(1-40) dimer explored by replica exchange molecular dynamics simulations.Quarterly intrinsic disorder digest (April-May-June, 2014).Solvent effects in the helix-coil transition model can explain the unusual biophysics of intrinsically disordered proteins.Stress-Triggered Phase Separation Is an Adaptive, Evolutionarily Tuned Response.Sequence- and Temperature-Dependent Properties of Unfolded and Disordered Proteins from Atomistic Simulations.Contribution of Water to Pressure and Cold Denaturation of Proteins.Protein plasticity driven by disorder and collapse governs the heterogeneous binding of CytR to DNA.Consistent Treatment of Hydrophobicity in Protein Lattice Models Accounts for Cold Denaturation
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P2860
Temperature-dependent solvation modulates the dimensions of disordered proteins.
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article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 21 March 2014
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Temperature-dependent solvation modulates the dimensions of disordered proteins.
@en
Temperature-dependent solvation modulates the dimensions of disordered proteins.
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type
label
Temperature-dependent solvation modulates the dimensions of disordered proteins.
@en
Temperature-dependent solvation modulates the dimensions of disordered proteins.
@nl
prefLabel
Temperature-dependent solvation modulates the dimensions of disordered proteins.
@en
Temperature-dependent solvation modulates the dimensions of disordered proteins.
@nl
P2093
P2860
P356
P1476
Temperature-dependent solvation modulates the dimensions of disordered proteins.
@en
P2093
Daniel Nettels
Hagen Hofmann
Jeetain Mittal
Madeleine B Borgia
René Wuttke
P2860
P304
P356
10.1073/PNAS.1313006111
P407
P577
2014-03-21T00:00:00Z