Reassessing random-coil statistics in unfolded proteins. - Wikidata - awgldk - TriplyDB

Reassessing random-coil statistics in unfolded proteins.

Reassessing random-coil statistics in unfolded proteins.

http://www.wikidata.org/entity/Q37487200

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Unfolded-state dynamics and structure of protein L characterized by simulation and experiment Amyloid beta-protein monomer folding: free-energy surfaces reveal alloform-specific differences Protein folding: then and now A backbone-based theory of protein folding A practical guide to small angle X-ray scattering (SAXS) of flexible and intrinsically disordered proteins Local order in the unfolded state: conformational biases and nearest neighbor interactions Order and disorder in intermediate filament proteins The effect of a DeltaK280 mutation on the unfolded state of a microtubule-binding repeat in Tau Slow unfolded-state structuring in Acyl-CoA binding protein folding revealed by simulation and experiment Confinement and Stabilization of Fyn SH3 Folding Intermediate Mimetics within the Cavity of the Chaperonin GroEL Demonstrated by Relaxation-Based NMR.Domain cooperativity in multidomain proteins: what can we learn from molecular alignment in anisotropic media?Structures, basins, and energies: a deconstruction of the Protein Coil Library.Creating novel protein scripts beyond natural alphabets Mapping protein collapse with single-molecule fluorescence and kinetic synchrotron radiation circular dichroism spectroscopy.Construction and comparison of the statistical coil states of unfolded and intrinsically disordered proteins from nearest-neighbor corrected conformational propensities of short peptides.On the importance of polar interactions for complexes containing intrinsically disordered proteins.Statistical coil model of the unfolded state: resolving the reconciliation problem.Building native protein conformation from highly approximate backbone torsion angles.Probing structural heterogeneities and fluctuations of nucleic acids and denatured proteins.Polymer properties of polythymine as revealed by translational diffusion Development of a technique for the investigation of folding dynamics of single proteins for extended time periods Importance of backbone and solvent properties for conformational dynamics in polypeptides.Hydrogen-bond driven loop-closure kinetics in unfolded polypeptide chains.Modulating native-like residual structure in the fully denatured state of photoactive yellow protein affects its refolding.Describing sequence-ensemble relationships for intrinsically disordered proteins.The kinetics of conformational fluctuations in an unfolded protein measured by fluorescence methods.Unusual compactness of a polyproline type II structure.Homogeneous and heterogeneous tertiary structure ensembles of amyloid-β peptides.Cooperative formation of native-like tertiary contacts in the ensemble of unfolded states of a four-helix protein Single-molecule Forster resonance energy transfer study of protein dynamics under denaturing conditions.Contribution of long-range interactions to the secondary structure of an unfolded globin The lipid-binding domain of wild type and mutant alpha-synuclein: compactness and interconversion between the broken and extended helix forms.A structural model for unfolded proteins from residual dipolar couplings and small-angle x-ray scattering.Measuring unfolding of proteins in the presence of denaturant using fluorescence correlation spectroscopy.Polyproline II propensities from GGXGG peptides reveal an anticorrelation with beta-sheet scales Chloroplastic Hsp100 chaperones ClpC2 and ClpD interact in vitro with a transit peptide only when it is located at the N-terminus of a protein.Are long-range structural correlations behind the aggregration phenomena of polyglutamine diseases?Universality in the timescales of internal loop formation in unfolded proteins and single-stranded oligonucleotides.Predicting most probable conformations of a given peptide sequence in the random coil state.Polyproline II conformation is one of many local conformational states and is not an overall conformation of unfolded peptides and proteins.

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P2860

Reassessing random-coil statistics in unfolded proteins.

http://www.wikidata.org/entity/Q37487200

description

article científic

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article scientifique

@fr

articolo scientifico

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artigo científico

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bilimsel makale

@tr

scientific article published on 16 August 2004

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Reassessing random-coil statistics in unfolded proteins.

@en

Reassessing random-coil statistics in unfolded proteins.

@nl

type

label

Reassessing random-coil statistics in unfolded proteins.

@en

Reassessing random-coil statistics in unfolded proteins.

@nl

prefLabel

Reassessing random-coil statistics in unfolded proteins.

@en

Reassessing random-coil statistics in unfolded proteins.

@nl

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PNAS.0404236101

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Reassessing random-coil statistics in unfolded proteins.

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George D Rose

http://www.w3.org/2001/XMLSchema#string

Nicholas C Fitzkee

http://www.w3.org/2001/XMLSchema#string

P2860

The Protein Data Bank

Levinthal's paradox

Polymer principles and protein folding

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

Raster3D: photorealistic molecular graphics

Stereochemistry of polypeptide chain configurations

Intrinsically disordered protein

CRYSOL– a Program to Evaluate X-ray Solution Scattering of Biological Macromolecules from Atomic Coordinates

The effect of the polyproline II (PPII) conformation on the denatured state entropy.

Ab initio prediction of protein structure using LINUS.

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12497-12502

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scholarly article

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10.1073/PNAS.0404236101

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2004-08-16T00:00:00Z

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15314216

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