Solvation energy in protein folding and binding (Q28307568)

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Language	Label	Description	Also known as
English	Solvation energy in protein folding and binding	scientific article

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scholarly article

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Solvation energy in protein folding and binding (English)

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protein folding

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author name string

D Eisenberg

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A D McLachlan

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language of work or name

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publication date

January 1986

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319

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6050

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199-203

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An analysis of incorrectly folded protein models. Implications for structure predictions.

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Some factors in the interpretation of protein denaturation

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Dynamics of proteins: elements and function

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Protein folding

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Computer simulation of protein folding

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Hydrophobicity of amino acid residues in globular proteins.

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Surface and inside volumes in globular proteins

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Affinities of amino acid side chains for solvent water

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Hydrophobic moments and protein structure

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Amino acid side-chain partition energies and distribution of residues in soluble proteins

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The apolar surface area of amino acids and its empirical correlation with hydrophobic free energy.

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Hydrophobic bonding and accessible surface area in proteins

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The interpretation of protein structures: Estimation of static accessibility

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Environment and exposure to solvent of protein atoms. Lysozyme and insulin

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Packing of α-helices: Geometrical constraints and contact areas

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Solvent accessible surface area and excluded volume in proteins. Analytical equations for overlapping spheres and implications for the hydrophobic effect

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Areas, volumes, packing and protein structure

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The Three-Dimensional Structure of a Phosphorylcholine-Binding Mouse Immunoglobulin Fab and the Nature of the Antigen Binding Site

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Pseudo-dynamic contact surface areas: estimation of apolar bonding

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Electrophoretic analysis of the unfolding of proteins by urea

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The helical hydrophobic moment: a measure of the amphiphilicity of a helix

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Analysis of membrane and surface protein sequences with the hydrophobic moment plot

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The hydrophobic moment detects periodicity in protein hydrophobicity

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Amphipathic analysis and possible formation of the ion channel in an acetylcholine receptor

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Calculations of electrostatic interactions in biological systems and in solutions

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Real-space refinement of the structure of hen egg-white lysozyme

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A structure-factor least-squares refinement procedure for macromolecular structures using constrainedandrestrained parameters

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Energy refinement of hen egg-white lysozyme

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based on heuristic

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