On the diversity of physicochemical environments experienced by identical ligands in binding pockets of unrelated proteins

Proteins: Structure, Function and Bioinformatics

Volumn 78, Issue 5, 2010, Pages 1120-1136

  Kahraman, Abdullah ^a,b   Morris, Richard J ^c   Laskowski, Roman A ^a   Favia, Angelo D ^d   Thornton, Janet M ^a  

^a WELLCOME TRUST SANGER INSTITUTE   (United Kingdom)

^b ETH ZURICH   (Switzerland)

^c JOHN INNES CENTRE   (United Kingdom)

^d ISTITUTO ITALIANO DI TECNOLOGIA   (Italy)

Author keywords

Cognate ligand; Electrostatics hydrophobicity; Molecular recognition; Noncomplementarity; Protein function; Protein ligand interaction; Redox potential

Indexed keywords

ADENOSINE TRIPHOSPHATE; NICOTINAMIDE ADENINE DINUCLEOTIDE; HEME; LIGAND; PROTEIN;

ARTICLE; BINDING SITE; CHEMICAL COMPOSITION; ELECTROCHEMICAL ANALYSIS; HYDROPHOBICITY; PHYSICAL CHEMISTRY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; ALGORITHM; ANIMAL; CHEMICAL STRUCTURE; CHEMISTRY; METABOLISM; PROTEIN CONFORMATION; PROTEIN FOLDING; STATIC ELECTRICITY;

ADENOSINE TRIPHOSPHATE; ALGORITHMS; ANIMALS; BINDING SITES; HEME; HYDROPHOBICITY; LIGANDS; MODELS, MOLECULAR; NAD; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEINS; STATIC ELECTRICITY;

EID: 77951245620     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22633     Document Type: Article

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