Improved affinity of engineered streptavidin for the Strep-tag II peptide is due to a fixed open conformation of the lid-like loop at the binding site

Protein Science

Volumn 11, Issue 4, 2002, Pages 883-893

  Korndörfer, Ingo P ^a   Skerra, Arne ^a  

^a TECHNICAL UNIVERSITY OF MUNICH   (Germany)

Author keywords

Biotin; Crystal structure; Protein engineering; Strep tag; Streptavidin

Indexed keywords

AMINO ACID; BIOTIN; LIGAND; MUTANT PROTEIN; PEPTIDE; STREPTAVIDIN;

ARTICLE; BINDING AFFINITY; BINDING SITE; COMPLEX FORMATION; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; ENTROPY; MUTATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN ENGINEERING; PROTEIN INTERACTION;

BINDING SITES; BINDING, COMPETITIVE; CHROMATOGRAPHY, AFFINITY; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ESCHERICHIA COLI; MODELS, MOLECULAR; MUTAGENESIS; OLIGOPEPTIDES; PROTEIN CONFORMATION; PROTEIN ENGINEERING; RECOMBINANT PROTEINS; STREPTAVIDIN;

EID: 0036129945     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.4150102     Document Type: Article

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