Introduction of histidine residues into avidin subunit interfaces allows pH-dependent regulation of quaternary structure and biotin binding

FEBS Letters

Volumn 555, Issue 3, 2003, Pages 449-454

  Nordlund, Henri R ^a   Hytönen, Vesa P ^a   Laitinen, Olli H ^b   Uotila, Sanna T H ^b   Niskanen, Einari A ^a   Savolainen, Janne ^a   Porkka, Eevaleena ^a   Kulomaa, Markku S ^a  

^a UNIVERSITY OF JYVÄSKYLÄ   (Finland)

^b UNIVERSITY OF EASTERN FINLAND   (Finland)

Author keywords

Avidin; pH dependence; Protein engineering

Indexed keywords

AVIDIN; BIOTIN; HISTIDINE; ISOLEUCINE; METHIONINE; MUTANT PROTEIN; VALINE;

AMINO ACID SUBSTITUTION; ARTICLE; BIOSENSOR; BIOTECHNOLOGY; COMPLEX FORMATION; FLUORESCENCE SPECTROSCOPY; PH; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN ENGINEERING; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN QUATERNARY STRUCTURE; REGULATORY MECHANISM; STRUCTURE ACTIVITY RELATION;

EID: 0347627526     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-5793(03)01302-4     Document Type: Article

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