Quantifying why urea is a protein denaturant, whereas glycine betaine is a protein stabilizer - Wikidata - wikimedia - TriplyDB

Quantifying why urea is a protein denaturant, whereas glycine betaine is a protein stabilizer

Quantifying why urea is a protein denaturant, whereas glycine betaine is a protein stabilizer

http://www.wikidata.org/entity/Q35345924

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Thermodynamics and solvent linkage of macromolecule-ligand interactions Osmotic Shock Induced Protein Destabilization in Living Cells and Its Reversal by Glycine Betaine.Kinetics and thermodynamics of membrane protein folding Quantifying the temperature dependence of glycine-betaine RNA duplex destabilization Interaction-component analysis of the hydration and urea effects on cytochrome c.Quantitative characterization of local protein solvation to predict solvent effects on protein structure.Toward an atomistic description of the urea-denatured state of proteins.Microscopic insights into the protein-stabilizing effect of trimethylamine N-oxide (TMAO)A hypothesis to reconcile the physical and chemical unfolding of proteins.Aspects of Weak Interactions between Folate and Glycine Betaine.Plant salt-tolerance mechanisms.Polymer collapse in miscible good solvents is a generic phenomenon driven by preferential adsorption.Quantitative assessments of the distinct contributions of polypeptide backbone amides versus side chain groups to chain expansion via chemical denaturation Synergy in protein-osmolyte mixtures.Chemical Interactions of Polyethylene Glycols (PEGs) and Glycerol with Protein Functional Groups: Applications to Effects of PEG and Glycerol on Protein Processes.Separating chemical and excluded volume interactions of polyethylene glycols with native proteins: Comparison with PEG effects on DNA helix formation.Its preferential interactions with biopolymers account for diverse observed effects of trehalose Urea-Water Solvation Forces on Prion Structures Solute's perspective on how trimethylamine oxide, urea, and guanidine hydrochloride affect water's hydrogen bonding ability Denaturation of RNA secondary and tertiary structure by urea: simple unfolded state models and free energy parameters account for measured m-values.Molecular mechanism for the preferential exclusion of TMAO from protein surfaces.Positioning the Intracellular Salt Potassium Glutamate in the Hofmeister Series by Chemical Unfolding Studies of NTL9.Quantifying functional group interactions that determine urea effects on nucleic acid helix formation.Infrared and Fluorescence Assessment of Protein Dynamics: From Folding to Function.Solvation free energy of the peptide group: its model dependence and implications for the additive-transfer free-energy model of protein stability Probing the protein-folding mechanism using denaturant and temperature effects on rate constants Distinctive solvation patterns make renal osmolytes diverse.Coupled enzyme reactions performed in heterogeneous reaction media: experiments and modeling for glucose oxidase and horseradish peroxidase in a PEG/citrate aqueous two-phase system.Experimental Atom-by-Atom Dissection of Amide-Amide and Amide-Hydrocarbon Interactions in H2O.Cosolute and Crowding Effects on a Side-By-Side Protein Dimer.TMAO-Protein Preferential Interaction Profile Determines TMAO's Conditional In Vivo Compatibility.Basis of Protein Stabilization by K Glutamate: Unfavorable Interactions with Carbon, Oxygen Groups.Single-molecule chemo-mechanical unfolding reveals multiple transition state barriers in a small single-domain protein.Probing the Action of Chemical Denaturant on an Intrinsically Disordered Protein by Simulation and Experiment.Using solutes and kinetics to probe large conformational changes in the steps of transcription initiation.Structure and dynamics of urea/water mixtures investigated by vibrational spectroscopy and molecular dynamics simulation.Quantifying additive interactions of the osmolyte proline with individual functional groups of proteins: comparisons with urea and glycine betaine, interpretation of m-values.Concluding remarks: Cum grano salis.Interactions of S-peptide analogue in aqueous urea and trimethylamine-N-oxide solutions: a molecular dynamics simulation study.The effect of urea on aqueous hydrophobic contact-pair interactions.

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P2860

Quantifying why urea is a protein denaturant, whereas glycine betaine is a protein stabilizer

http://www.wikidata.org/entity/Q35345924

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2011 nî lūn-bûn

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2011 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

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2011 թվականի սեպտեմբերին հրատարակված գիտական հոդված

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2011年論文

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2011年論文

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Quantifying why urea is a prot ...... etaine is a protein stabilizer

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Quantifying why urea is a prot ...... etaine is a protein stabilizer

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Quantifying why urea is a prot ...... etaine is a protein stabilizer

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

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Quantifying why urea is a prot ...... etaine is a protein stabilizer

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Emily J Guinn

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Laurel M Pegram

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M Thomas Record

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Michael W Capp

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Michelle N Pollock

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P2860

How Hofmeister ion interactions affect protein stability

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

Urea, but not guanidinium, destabilizes proteins by forming hydrogen bonds to the peptide group.

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

Urea-amide preferential interactions in water: quantitative comparison of model compound data with biopolymer results using water accessible surface areas.

Why Hofmeister effects of many salts favor protein folding but not DNA helix formation.

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

Betaine can eliminate the base pair composition dependence of DNA melting.

Backbone and side-chain contributions in protein denaturation by urea.

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