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Volumn 972, Issue 1, 2002, Pages 61-75
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Reversed-phase liquid chromatography as a tool in the determination of the hydrophilicity/hydrophobicity of amino acid side-chains at a ligand-receptor interface in the presence of different aqueous environments: II. Effect of varying peptide ligand hydrophobicity
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Author keywords
Amino acids; Hydrophilicity; Hydrophobicity; Interfaces, ligand receptor; Ligand receptor interfaces; Peptides
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Indexed keywords
AMINO ACIDS;
HYDROPHILICITY;
HYDROPHOBICITY;
PH EFFECTS;
POLARIZATION;
PROTEINS;
PEPTIDES;
LIQUID CHROMATOGRAPHY;
ALANINE;
AMINO ACID;
LEUCINE;
LIGAND;
MUTANT PROTEIN;
PEPTIDE DERIVATIVE;
RECEPTOR PROTEIN;
SODIUM CHLORIDE;
ALPHA HELIX;
AMINO ACID SEQUENCE;
AMINO ACID SUBSTITUTION;
AQUEOUS SOLUTION;
ARTICLE;
BINDING SITE;
EXPERIMENTAL MODEL;
HYDROPHILICITY;
HYDROPHOBICITY;
LIGAND BINDING;
MOLECULAR INTERACTION;
PH;
POLARIZATION;
PRIORITY JOURNAL;
PROTEIN DOMAIN;
REVERSED PHASE LIQUID CHROMATOGRAPHY;
SURFACE CHARGE;
AMINO ACIDS;
CHROMATOGRAPHY, HIGH PRESSURE LIQUID;
LIGANDS;
PEPTIDES;
RECEPTORS, CELL SURFACE;
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EID: 0037183709
PISSN: 00219673
EISSN: None
Source Type: Journal
DOI: 10.1016/S0021-9673(02)00356-4 Document Type: Article |
Times cited : (12)
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References (34)
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