In pursuit of virtual lead optimization: Pruning ensembles of receptor structures for increased efficiency and accuracy during docking

Proteins: Structure, Function and Bioinformatics

Volumn 75, Issue 1, 2009, Pages 62-74

  Bolstad, Erin S D ^a   Anderson, Amy C ^a  

^a UNIVERSITY OF CONNECTICUT   (United States)

Author keywords

Crystal structure; DHFR; Docking; Ensembles; Homology models; Protein flexibility; Solution structure

Indexed keywords

ACETYLCHOLINESTERASE; DOCKING PROTEIN; PROTEINASE; VIRUS ENZYME;

ARTICLE; COMPUTER MODEL; GEOMETRY; HUMAN IMMUNODEFICIENCY VIRUS 1; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN STRUCTURE;

AMINO ACID SEQUENCE; CLUSTER ANALYSIS; COMPUTATIONAL BIOLOGY; COMPUTER SIMULATION; CONSERVED SEQUENCE; DRUG DISCOVERY; LIGANDS; MODELS, MOLECULAR; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; TETRAHYDROFOLATE DEHYDROGENASE;

HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 65249157200     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22214     Document Type: Article

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