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 - sprookjes - yvandenbroek - TriplyDB

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

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

http://www.wikidata.org/entity/Q28364507

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Recent applications of Kirkwood-Buff theory to biological systems Biomolecular electrostatics and solvation: a computational perspective Protein Stabilization and the Hofmeister Effect: The Role of Hydrophobic Solvation Exploring early stages of the chemical unfolding of proteins at the proteome scale Insights into the structure and function of HV1 from a meta-analysis of mutation studies Kinetics and thermodynamics of membrane protein folding The addition of 2,2,2-trifluoroethanol prevents the aggregation of guanidinium around protein and impairs its denaturation ability: a molecular dynamics simulation study.Structural characterization of apomyoglobin self-associated species in aqueous buffer and urea solution.Counteraction of urea-induced protein denaturation by trimethylamine N-oxide: a chemical chaperone at atomic resolution.Why Hofmeister effects of many salts favor protein folding but not DNA helix formation.Hydration of guanidinium depends on its local environment.Protein stability in mixed solvents: a balance of contact interaction and excluded volume Quantitative assessments of the distinct contributions of polypeptide backbone amides versus side chain groups to chain expansion via chemical denaturation The molecular basis for the chemical denaturation of proteins by urea.Partitioning of atmospherically relevant ions between bulk water and the water/vapor interface Glucose interactions with a model peptide.Quantifying why urea is a protein denaturant, whereas glycine betaine is a protein stabilizer The interaction of guanidinium ions with a model peptide.Anatomy of energetic changes accompanying urea-induced protein denaturation.Its preferential interactions with biopolymers account for diverse observed effects of trehalose Lack of Dependence of the Sizes of the Mesoscopic Protein Clusters on Electrostatics Protein Stabilization and Enzyme Activation in Ionic Liquids: Specific Ion Effects Preferential interactions between small solutes and the protein backbone: a computational analysis Quantifying functional group interactions that determine urea effects on nucleic acid helix formation.Urea orientation at protein surfaces.Small-angle X-ray scattering of reduced ribonuclease A: effects of solution conditions and comparisons with a computational model of unfolded proteins Investigation of cosolute-protein preferential interaction coefficients: new insight into the mechanism by which arginine inhibits aggregation.Preferential interactions of guanidinum ions with aromatic groups over aliphatic groups.Biopharmaceutical liquid formulation: a review of the science of protein stability and solubility in aqueous environments.Sulfate anion stabilization of native ribonuclease A both by anion binding and by the Hofmeister effect.Late steps in the formation of E. coli RNA polymerase-lambda P R promoter open complexes: characterization of conformational changes by rapid [perturbant] upshift experiments.Preferential interactions of trehalose, L-arginine.HCl and sodium chloride with therapeutically relevant IgG1 monoclonal antibodies.Compatible solute influence on nucleic acids: many questions but few answers.The efficiency of different salts to screen charge interactions in proteins: a Hofmeister effect?Effects of osmolytes on RNA secondary and tertiary structure stabilities and RNA-Mg2+ interactions.Introductory lecture: interpreting and predicting Hofmeister salt ion and solute effects on biopolymer and model processes using the solute partitioning model Use of urea and glycine betaine to quantify coupled folding and probe the burial of DNA phosphates in lac repressor-lac operator binding.Formation of a wrapped DNA-protein interface: experimental characterization and analysis of the large contributions of ions and water to the thermodynamics of binding IHF to H' DNA.Thermodynamic origin of hofmeister ion effects Nonspecific DNA binding and bending by HUαβ: interfaces of the three binding modes characterized by salt-dependent thermodynamics.

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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

http://www.wikidata.org/entity/Q28364507

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Thermodynamics of interactions ...... water-accessible surface area

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Protein Science

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Thermodynamics of interactions ...... water-accessible surface area

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How Hofmeister ion interactions affect protein stability

The stabilization of proteins by osmolytes

Crystal structure of human serum albumin at 2.5 A resolution

Coupling of local folding to site-specific binding of proteins to DNA

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

Preferential hydration of bovine serum albumin in polyhydric alcohol-water mixtures.

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

Thermodynamic stoichiometries of participation of water, cations and anions in specific and non-specific binding of lac repressor to DNA. Possible thermodynamic origins of the "glutamate effect" on protein-DNA interactions.

Use of liquid hydrocarbon and amide transfer data to estimate contributions to thermodynamic functions of protein folding from the removal of nonpolar and polar surface from water.

Interpretation of preferential interaction coefficients of nonelectrolytes and of electrolyte ions in terms of a two-domain model

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