about
Classification of intrinsically disordered regions and proteinsPhysicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)Residual structure in unfolded proteinsRelating sequence encoded information to form and function of intrinsically disordered proteinsWhen fast is better: protein folding fundamentals and mechanisms from ultrafast approachesEntropic stabilization of proteins by TMAODescribing sequence-ensemble relationships for intrinsically disordered proteins.Solubility and aggregation of Gly(5) in water.Residual structures, conformational fluctuations, and electrostatic interactions in the synergistic folding of two intrinsically disordered proteins.Quantitative assessments of the distinct contributions of polypeptide backbone amides versus side chain groups to chain expansion via chemical denaturationRegulation and aggregation of intrinsically disordered peptidesForce field-dependent solution properties of glycine oligomersScaling properties of glycine-rich sequences in guanidine hydrochloride solutions.Polymer scaling laws of unfolded and intrinsically disordered proteins quantified with single-molecule spectroscopyConformational properties of polyglutamine sequences in guanidine hydrochloride solutionsSmall-angle X-ray scattering and single-molecule FRET spectroscopy produce highly divergent views of the low-denaturant unfolded state.Reducing the dimensionality of the protein-folding search problem.Long range recognition and selection in IDPs: the interactions of the C-terminus of p53Protein collapse driven against solvation free energy without H-bonds.A quantitative measure for protein conformational heterogeneityMeandering Down the Energy Landscape of Protein Folding: Are We There Yet?Importance of Hydrophilic Hydration and Intramolecular Interactions in the Thermodynamics of Helix-Coil Transition and Helix-Helix Assembly in a Deca-Alanine Peptide.How, when and why proteins collapse: the relation to folding.Studies of protein folding and dynamics using single molecule fluorescence spectroscopy.The roughness of the protein energy landscape results in anomalous diffusion of the polypeptide backbone.Handedness preference and switching of peptide helices. Part II: Helices based on noncoded α-amino acids.Chain collapse of an amyloidogenic intrinsically disordered protein.The loop hypothesis: contribution of early formed specific non-local interactions to the determination of protein folding pathways.Intrinsic α helix propensities compact hydrodynamic radii in intrinsically disordered proteins.Perplexing cooperative folding and stability of a low-sequence complexity, polyproline 2 protein lacking a hydrophobic core.Long-range modulation of chain motions within the intrinsically disordered transactivation domain of tumor suppressor p53.Solvation Thermodynamics of Oligoglycine with Respect to Chain Length and Flexibility.The unsolved "solved-problem" of protein foldingThe contribution of electrostatic interactions to the collapse of oligoglycine in water.Tryptophan stabilizes His-heme loops in the denatured state only when it is near a loop endAntifragility and Tinkering in Biology (and in Business) Flexibility Provides an Efficient Epigenetic Way to Manage Risk.Confinement-dependent friction in peptide bundlesTuning the Flexibility of Glycine-Serine Linkers To Allow Rational Design of Multidomain Proteins.Peptide Solubility Limits: Backbone and Side-Chain Interactions.Intramolecular Interactions Overcome Hydration to Drive the Collapse Transition of Gly15.
P2860
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P2860
description
2011 nî lūn-bûn
@nan
2011 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի ապրիլին 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
Backbone-driven collapse in unfolded protein chains.
@ast
Backbone-driven collapse in unfolded protein chains.
@en
type
label
Backbone-driven collapse in unfolded protein chains.
@ast
Backbone-driven collapse in unfolded protein chains.
@en
prefLabel
Backbone-driven collapse in unfolded protein chains.
@ast
Backbone-driven collapse in unfolded protein chains.
@en
P2093
P1476
Backbone-driven collapse in unfolded protein chains.
@en
P2093
Christopher M Johnson
Daniel P Teufel
Hannes Neuweiler
Jenifer K Lum
P304
P356
10.1016/J.JMB.2011.03.066
P407
P577
2011-04-08T00:00:00Z