Anatomy of energetic changes accompanying urea-induced protein denaturation. - Wikidata - wikimedia - TriplyDB

Anatomy of energetic changes accompanying urea-induced protein denaturation.

Anatomy of energetic changes accompanying urea-induced protein denaturation.

http://www.wikidata.org/entity/Q36024166

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Residual structure in unfolded proteins Urea denatured state ensembles contain extensive secondary structure that is increased in hydrophobic proteins The Role of Zn 2+ on the Structure and Stability of Murine Adenosine Deaminase †The protein folding problem Exploring early stages of the chemical unfolding of proteins at the proteome scale Heat, Acid and Chemically Induced Unfolding Pathways, Conformational Stability and Structure-Function Relationship in Wheat α-Amylase Entropic stabilization of proteins by TMAO Urea, but not guanidinium, destabilizes proteins by forming hydrogen bonds to the peptide group.Analysis of repeat-protein folding using nearest-neighbor statistical mechanical models Toward an atomistic description of the urea-denatured state of proteins.A hypothesis to reconcile the physical and chemical unfolding of proteins.Trimethylamine N-oxide influence on the backbone of proteins: an oligoglycine model.Backbone additivity in the transfer model of protein solvation.Solubility and aggregation of Gly(5) in water.Quantitative comparison of villin headpiece subdomain simulations and triplet-triplet energy transfer experiments Thermodynamic perspective on the dock-lock growth mechanism of amyloid fibrils.Investigating and Annotating the Role of Citation in Biomedical Full-Text Articles The structural basis of urea-induced protein unfolding in β-catenin Quantitative assessments of the distinct contributions of polypeptide backbone amides versus side chain groups to chain expansion via chemical denaturation Benchmarking all-atom simulations using hydrogen exchange.Backbone and side-chain contributions in protein denaturation by urea.Protein denaturants at aqueous-hydrophobic interfaces: self-consistent correlation between induced interfacial fluctuations and denaturant stability at the interface.Collapse kinetics and chevron plots from simulations of denaturant-dependent folding of globular proteins.Peptide conformational preferences in osmolyte solutions: transfer free energies of decaalanine.Chirality-selected phase behaviour in ionic polypeptide complexes Separation of preferential interaction and excluded volume effects on DNA duplex and hairpin stability.Quantifying why urea is a protein denaturant, whereas glycine betaine is a protein stabilizer Manifestations of native topology in the denatured state ensemble of Rhodopseudomonas palustris cytochrome c'.A thermodynamic definition of protein domains Structural origins of misfolding propensity in the platelet adhesive von Willebrand factor A1 domain.Lack of Dependence of the Sizes of the Mesoscopic Protein Clusters on Electrostatics Solute's perspective on how trimethylamine oxide, urea, and guanidine hydrochloride affect water's hydrogen bonding ability The N-terminal capping propensities of the D-helix modulate the allosteric activation of the Escherichia coli cAMP receptor protein.Assessing the solvent-dependent surface area of unfolded proteins using an ensemble model Molecular mechanism for the preferential exclusion of TMAO from protein surfaces.Transcriptional responses of uropathogenic Escherichia coli to increased environmental osmolality caused by salt or urea Reducing the dimensionality of the protein-folding search problem.Properties of hydrophobic free energy found by gas-liquid transfer Protein collapse driven against solvation free energy without H-bonds.Dimensions, energetics, and denaturant effects of the protein unstructured state

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P2860

Anatomy of energetic changes accompanying urea-induced protein denaturation.

http://www.wikidata.org/entity/Q36024166

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Anatomy of energetic changes accompanying urea-induced protein denaturation.

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Anatomy of energetic changes accompanying urea-induced protein denaturation.

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Anatomy of energetic changes accompanying urea-induced protein denaturation.

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

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Anatomy of energetic changes accompanying urea-induced protein denaturation

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D Wayne Bolen

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Luis Marcelo F Holthauzen

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P2860

Mixed osmolytes: the degree to which one osmolyte affects the protein stabilizing ability of another

The interpretation of protein structures: estimation of static accessibility

Some factors in the interpretation of protein denaturation

Thermodynamics of interactions of urea and guanidinium salts with protein surface: relationship between solute effects on protein processes and changes in water-accessible surface area

Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding

A naturally occurring protective system in urea-rich cells: mechanism of osmolyte protection of proteins against urea denaturation.

Predicting the energetics of osmolyte-induced protein folding/unfolding.

Protein stability in mixed solvents: a balance of contact interaction and excluded volume

Protein stabilization by naturally occurring osmolytes.

The molecular basis for the chemical denaturation of proteins by urea.

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