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Volumn , Issue , 1998, Pages 362-373
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Molecular anchors with large stability gaps ensure linear binding free energy relationships for hydrophobic substituents.
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Author keywords
[No Author keywords available]
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Indexed keywords
FK 506 BINDING PROTEIN;
IMMUNOPHILIN;
LIGAND;
LYSOZYME;
TACROLIMUS;
ARTICLE;
BACTERIOPHAGE T4;
BINDING SITE;
CHEMICAL STRUCTURE;
CHEMISTRY;
COMPUTER PROGRAM;
COMPUTER SIMULATION;
CONFORMATION;
DRUG DESIGN;
ENZYME ACTIVE SITE;
ENZYMOLOGY;
HYDROGEN BOND;
METABOLISM;
PROTEIN CONFORMATION;
THERMODYNAMICS;
ALLOSTERIC SITE;
BACTERIOPHAGE T4;
BINDING SITES;
CATALYTIC DOMAIN;
COMPUTER SIMULATION;
DRUG DESIGN;
HYDROGEN BONDING;
IMMUNOPHILINS;
LIGANDS;
MODELS, MOLECULAR;
MOLECULAR CONFORMATION;
MURAMIDASE;
PROTEIN CONFORMATION;
SOFTWARE;
TACROLIMUS;
TACROLIMUS BINDING PROTEINS;
THERMODYNAMICS;
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EID: 0031635564
PISSN: None
EISSN: None
Source Type: Journal
DOI: None Document Type: Article |
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Times cited : (5)
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References (0)
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