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Solvation energy in protein folding and binding
scientific article
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instance of
scholarly article
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title
Solvation energy in protein folding and binding
(English)
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main subject
protein folding
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author name string
D Eisenberg
series ordinal
1
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A D McLachlan
series ordinal
2
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language of work or name
English
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publication date
January 1986
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stated in
PubMed
published in
Nature
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volume
319
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page(s)
199-203
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issue
6050
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cites work
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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Crossref
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Dynamics of proteins: elements and function
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stated in
Crossref
reference URL
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7 January 2021
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Protein folding
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1038%2F319199A0
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7 January 2021
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Computer simulation of protein folding
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based on heuristic
inferred from DOI database lookup
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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Crossref
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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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Crossref
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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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Crossref
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7 January 2021
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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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7 January 2021
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inferred from DOI database lookup
Real-space refinement of the structure of hen egg-white lysozyme
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Crossref
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7 January 2021
based on heuristic
inferred from DOI database lookup
A structure-factor least-squares refinement procedure for macromolecular structures using constrainedandrestrained parameters
1 reference
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Crossref
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https://api.crossref.org/works/10.1038%2F319199A0
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7 January 2021
based on heuristic
inferred from DOI database lookup
Energy refinement of hen egg-white lysozyme
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1038%2F319199A0
retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
Identifiers
DOI
10.1038/319199A0
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1618550
Dimensions Publication ID
1020743092
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OpenCitations bibliographic resource ID
1618550
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1618550
PubMed ID
3945310
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1618550
Springer Nature article ID
10.1038/319199a0
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