Spectral and metal-binding properties of three single-point tryptophan mutants of the human transferrin N-lobe

Biochemical Journal

Volumn 354, Issue 2, 2001, Pages 423-429

  He, Q Y ^a   Mason, A B ^a   Lyons, B A ^a   Tam, B M ^a   Nguyen, V ^a   MacGillivray, R T A ^a   Woodworth, R C ^a  

^a UNIVERSITY OF VERMONT   (United States)

Author keywords

Fluorescence; Kinetics; Metal protein; NMR; Paramagnetic effect

Indexed keywords

TRANSFERRIN; TRYPTOPHAN;

AMINO ACID SEQUENCE; ARTICLE; BINDING AFFINITY; HUMAN; IRON TRANSPORT; POINT MUTATION; PRIORITY JOURNAL; PROTEIN CONFORMATION; STRUCTURE ACTIVITY RELATION; TRANSFERRIN BLOOD LEVEL;

AMINO ACID SUBSTITUTION; ANIMALS; CELLS, CULTURED; COBALT; CRICETINAE; HISTIDINE; HUMANS; IRON; MAGNETIC RESONANCE SPECTROSCOPY; METALS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; POINT MUTATION; PROTEIN CONFORMATION; PROTEIN SUBUNITS; SPECTROMETRY, FLUORESCENCE; SPECTROPHOTOMETRY, ATOMIC; SPECTROPHOTOMETRY, ULTRAVIOLET; STRUCTURE-ACTIVITY RELATIONSHIP; TRANSFERRIN; TRYPTOPHAN;

EID: 0035282222     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/0264-6021:3540423     Document Type: Article

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