Protein folding: defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteins. - Wikidata - awgldk - TriplyDB

Protein folding: defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteins.

Protein folding: defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteins.

http://www.wikidata.org/entity/Q30981967

about

Relevance of weak flavin binding in human D-amino acid oxidase (NZ)CH...O Contacts assist crystallization of a ParB-like nuclease Significant stabilization of ribonuclease A by additive effects The protein folding problem On the precision of experimentally determined protein folding rates and phi-values Nonequilibrium single molecule protein folding in a coaxial mixer Development and Application of a High Throughput Protein Unfolding Kinetic Assay Control of human VDAC-2 scaffold dynamics by interfacial tryptophans is position specific.Mutational investigation of protein folding transition states by Phi-value analysis and beyond: lessons from SH3 domain folding.On the polymer physics origins of protein folding thermodynamics.Assessing the effect of dynamics on the closed-loop protein-folding hypothesis A miniaturized technique for assessing protein thermodynamics and function using fast determination of quantitative cysteine reactivity.Circular dichroism in protein folding studies.A comparison of the folding kinetics of a small, artificially selected DNA aptamer with those of equivalently simple naturally occurring proteins.A comprehensive database of verified experimental data on protein folding kinetics.Golden triangle for folding rates of globular proteins.SeqRate: sequence-based protein folding type classification and rates prediction Relation of completeness of reporting of health research to journals' endorsement of reporting guidelines: systematic review Biological effects of the hypomagnetic field: An analytical review of experiments and theories Predicting protein folding rates using the concept of Chou's pseudo amino acid composition.Investigation of an anomalously accelerating substitution in the folding of a prototypical two-state protein.Identification of the minimal protein-folding nucleus through loop-entropy perturbations The inverted chevron plot measured by NMR relaxation reveals a native-like unfolding intermediate in acyl-CoA binding protein High-throughput single-molecule optofluidic analysis.The core trisaccharide of an N-linked glycoprotein intrinsically accelerates folding and enhances stability Modulation of folding energy landscape by charge-charge interactions: linking experiments with computational modeling RNA molecules with conserved catalytic cores but variable peripheries fold along unique energetically optimized pathways.Unfolding analysis of the mature and unprocessed forms of Bacillus licheniformis γ-glutamyltranspeptidase Physical limits of cells and proteomes A Residue Quartet in the Extracellular Domain of the Prolactin Receptor Selectively Controls Mitogen-activated Protein Kinase Signaling Cooperative folding of a polytopic α-helical membrane protein involves a compact N-terminal nucleus and nonnative loops.Scope and utility of hydrogen exchange as a tool for mapping landscapes On the role of structural class of a protein with two-state folding kinetics in determining correlations between its size, topology, and folding rate.Unique fluorophores in the dimeric archaeal histones hMfB and hPyA1 reveal the impact of nonnative structure in a monomeric kinetic intermediate BPPred: a Web-based computational tool for predicting biophysical parameters of proteins.Methods for the accurate estimation of confidence intervals on protein folding phi-values Repeat-protein folding: new insights into origins of cooperativity, stability, and topology.One-dimensional barrier-preserving free-energy projections of a beta-sheet miniprotein: new insights into the folding process.Restrictions to protein folding determined by the protein size.Computational tools help improve protein stability but with a solubility tradeoff.

P2860

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P2860

Protein folding: defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteins.

http://www.wikidata.org/entity/Q30981967

description

2005 nî lūn-bûn

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2005 թուականի Փետրուարին հրատարակուած գիտական յօդուած

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2005 թվականի փետրվարին հրատարակված գիտական հոդված

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2005年の論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年论文

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Protein folding: defining a "s ...... ata set of two-state proteins.

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Protein folding: defining a "s ...... ata set of two-state proteins.

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Protein folding: defining a "s ...... ata set of two-state proteins.

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Protein folding: defining a "s ...... ata set of two-state proteins.

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Protein folding: defining a "s ...... ata set of two-state proteins.

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Protein folding: defining a "s ...... ata set of two-state proteins.

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P1433

Protein Science

P1476

Protein folding: defining a "s ...... ata set of two-state proteins.

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P2093

Alan R Davidson

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

Alexis Vallée-Bélisle

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

Andrew G Brown

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

David Wildes

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

Diane Bona

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

Erik J Miller

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

Ewan R G Main

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

Fabrizio Chiti

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

Flemming M Poulsen

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

Ingo Ruczinski

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

P2860

Different folding transition states may result in the same native structure

Structural changes in the transition state of protein folding: alternative interpretations of curved chevron plots

Is an intermediate state populated on the folding pathway of ubiquitin?

Apparent Debye-Huckel electrostatic effects in the folding of a simple, single domain protein

Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants

Understanding protein hydrogen bond formation with kinetic H/D amide isotope effects.

Studies of Pseudomonas aeruginosa azurin mutants: cavities in beta-barrel do not affect refolding speed.

Mutagenesis of a buried polar interaction in an SH3 domain: sequence conservation provides the best prediction of stability effects.

The folding kinetics and thermodynamics of the Fyn-SH3 domain.

Folding dynamics of the src SH3 domain.

P304

602-616

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scholarly article

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10.1110/PS.041205405

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3

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P478

14

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Pernilla Wittung-Stafshede

Arash Zarrine-Afsar

Birthe B Kragelund

Claire T. Friel

Daniel P Raleigh

Francesco Bemporad

P577

2005-02-02T00:00:00Z

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227725102

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15689503

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protein folding

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2279278

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