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Energetics of hydrogen bonding in proteins: a model compound study

Energetics of hydrogen bonding in proteins: a model compound study

http://www.wikidata.org/entity/Q30444039

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Two different proteins that compete for binding to thrombin have opposite kinetic and thermodynamic profiles Thermodynamics and solvent linkage of macromolecule-ligand interactions The contribution of polar group burial to protein stability is strongly context-dependent Synergistic Inhibition of Protein Fibrillation by Proline and Sorbitol: Biophysical Investigations Characterizing the role of ensemble modulation in mutation-induced changes in binding affinity Exploring the impact of polyproline II (PII) conformational bias on the binding of peptides to the SEM-5 SH3 domain.Thermodynamic propensities of amino acids in the native state ensemble: implications for fold recognition.Solvation in protein (un)folding of melittin tetramer-monomer transition.Quantitative assessment of protein structural models by comparison of H/D exchange MS data with exchange behavior accurately predicted by DXCOREX.The structure of a glycogen phosphorylase glucopyranose spirohydantoin complex at 1.8 A resolution and 100 K: the role of the water structure and its contribution to binding Analysis of the "thermodynamic information content" of a Homo sapiens structural database reveals hierarchical thermodynamic organization.Heat Capacity Changes for Transition-State Analogue Binding and Catalysis with Human 5'-Methylthioadenosine Phosphorylase.Local conformational fluctuations can modulate the coupling between proton binding and global structural transitions in proteins.Hydrogen bonding stabilizes globular proteins.Molecular hydrogels from bolaform amino acid derivatives: a structure-properties study based on the thermodynamics of gel solubilization.Binding-linked protonation of a DNA minor-groove agent Amyloid fibrillation of insulin under water-limited conditions Free energetics of arginine permeation into model DMPC lipid bilayers: coupling of effective counterion concentration and lateral bilayer dimensions Binding sites in Escherichia coli dihydrofolate reductase communicate by modulating the conformational ensemble Hydrodynamic Radii of Intrinsically Disordered Proteins Determined from Experimental Polyproline II Propensities.Thermodynamic environments in proteins: fundamental determinants of fold specificity Hydrogen-bonding classes in proteins and their contribution to the unfolding reaction Structures of active site histidine mutants of IIIGlc, a major signal-transducing protein in Escherichia coli. Effects on the mechanisms of regulation and phosphoryl transfer.Sequence specific and high affinity recognition of 5'-ACGCGT-3' by rationally designed pyrrole-imidazole H-pin polyamides: thermodynamic and structural studies Structural energetics of protein-carbohydrate interactions: Insights derived from the study of lysozyme binding to its natural saccharide inhibitors.Multiple helical conformations of the helix-turn-helix region revealed by NOE-restrained MD simulations of tryptophan aporepressor, TrpR.Intrinsic α helix propensities compact hydrodynamic radii in intrinsically disordered proteins.Targeting human telomeric G-quadruplex DNA with oxazole-containing macrocyclic compounds.Network rigidity at finite temperature: relationships between thermodynamic stability, the nonadditivity of entropy, and cooperativity in molecular systems Contribution of charged groups to the enthalpic stabilization of the folded states of globular proteins.Thermodynamic analysis of the effect of selective monodeamidation at asparagine 67 in ribonuclease A.Temperature effects on the hydrodynamic radius of the intrinsically disordered N-terminal region of the p53 protein.Systematic interaction analysis of human lipocalin-type prostaglandin D synthase with small lipophilic ligands.How are hydrogen bonds modified by metal binding?Binding Affinity of Metal Ions to the CD11b A-domain Is Regulated by Integrin Activation and Ligands.Mutational analysis of m-values as a strategy to identify cold-resistant substructures of the protein ensemble.Nature and Strength of the Inner-Core H⋅⋅⋅H Interactions in Porphyrinoids.Energetic Components of Cooperative Protein Folding

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P2860

Energetics of hydrogen bonding in proteins: a model compound study

http://www.wikidata.org/entity/Q30444039

description

1996 nî lūn-bûn

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1996 թուականի Յուլիսին հրատարակուած գիտական յօդուած

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1996 թվականի հուլիսին հրատարակված գիտական հոդված

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1996年の論文

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1996年論文

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1996年論文

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1996年論文

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1996年論文

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1996年論文

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1996年论文

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Energetics of hydrogen bonding in proteins: a model compound study

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Energetics of hydrogen bonding in proteins: a model compound study

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Energetics of hydrogen bonding in proteins: a model compound study

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Energetics of hydrogen bonding in proteins: a model compound study

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Protein Science

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Energetics of hydrogen bonding in proteins: a model compound study

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Habermann SM

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Murphy KP

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P2860

Toward a simplification of the protein folding problem: a stabilizing polyalanine alpha-helix engineered in T4 lysozyme

Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala-->Ser and Val-->Thr substitutions in T4 lysozyme

Areas, volumes, packing and protein structure

Contribution of hydration and non-covalent interactions to the heat capacity effect on protein unfolding.

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.

Extracting hydrophobic free energies from experimental data: relationship to protein folding and theoretical models.

Calorimetric determination of the enthalpy change for the alpha-helix to coil transition of an alanine peptide in water.

An equation of state describing hydrophobic interactions.

Enthalpy of hydrogen bond formation in a protein-ligand binding reaction

Thermodynamics of structural stability and cooperative folding behavior in proteins.

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1229-1239

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scholarly article

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10.1002/PRO.5560050702

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7

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5

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8819156

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2143469

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