Analysis of novel streptavidin-binding peptides, identified using a phage display library, shows that amino acids external to a perfectly conserved consensus sequence and to the presented peptides contribute to binding

Molecular Diversity

Volumn 1, Issue 4, 1996, Pages 241-246

  Caparon, Maire H ^a   De Ciechi, Pamela A ^a   Devine, Catherine S ^a   Olins, Peter O ^a,b   Lee, Stephen C ^a  

^a MONSANTO COMPANY   (United States)

^b BAXTER HEALTHCARE CORPORATION   (United States)

Author keywords

Peptide library; Peptide modelling; Phage display; Streptavidin

Indexed keywords

BACTERIAL PROTEIN; OLIGOPEPTIDE; PEPTIDE LIBRARY; STREPTAVIDIN;

AMINO ACID SEQUENCE; ARTICLE; BINDING SITE; CHEMISTRY; CONSENSUS SEQUENCE; DIRECTED MOLECULAR EVOLUTION; ESCHERICHIA COLI; GENETICS; IN VITRO STUDY; INOVIRIDAE; METABOLISM; METHODOLOGY; NUCLEOTIDE SEQUENCE; PROTEIN BINDING;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BINDING SITES; CONSENSUS SEQUENCE; CONSERVED SEQUENCE; DIRECTED MOLECULAR EVOLUTION; ESCHERICHIA COLI; INOVIRUS; OLIGOPEPTIDES; PEPTIDE LIBRARY; PROTEIN BINDING; STREPTAVIDIN;

EID: 0030202293     PISSN: 13811991     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF01715528     Document Type: Article

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