Site-directed mutagenesis of either the highly conserved Trp-22 or the moderately conserved Trp-95 to a large, hydrophobic residue reduces the thermodynamic stability of a spectrin repeating unit

Journal of Biological Chemistry

Volumn 272, Issue 34, 1997, Pages 21052-21059

  Pantazatos, Dennis P ^a   MacDonald, Ruby I ^a  

^a NORTHWESTERN UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

SPECTRIN;

ALPHA HELIX; ANIMAL CELL; ARTICLE; CIRCULAR DICHROISM; CYTOSKELETON; HYDROPHOBICITY; NONHUMAN; PEPTIDE SYNTHESIS; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STABILITY; SEQUENCE HOMOLOGY; SITE DIRECTED MUTAGENESIS; TANDEM REPEAT; THERMODYNAMICS;

AMINO ACID SEQUENCE; ANIMALS; CHICKENS; CIRCULAR DICHROISM; DIMERIZATION; HUMANS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PEPTIDES; PROTEIN DENATURATION; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; SCATTERING, RADIATION; SOLUBILITY; SPECTRIN; SPECTROMETRY, FLUORESCENCE; SPECTROPHOTOMETRY, ULTRAVIOLET; STRUCTURE-ACTIVITY RELATIONSHIP; THERMODYNAMICS; TRYPTOPHAN; UREA;

ANIMALIA; GALLUS GALLUS;

EID: 0030772373     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.272.34.21052     Document Type: Article

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