Role of tryptophan-63 of the kringle 2 domain of tissue-type plasminogen activator in its thermal stability, folding, and ligand binding properties

Biochemistry

Volumn 36, Issue 25, 1997, Pages 7652-7663

  Chang, Yuan ^a   Zajicek, Jaroslav ^a   Castellino, Francis J ^a  

^a UNIVERSITY OF NOTRE DAME   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

MUTANT PROTEIN; POLYPEPTIDE; TISSUE PLASMINOGEN ACTIVATOR; TRYPTOPHAN;

ARTICLE; BLOOD CLOT LYSIS; BLOOD CLOTTING; ENDOMYCETALES; GENETIC ENGINEERING; KRINGLE DOMAIN; LIGAND BINDING; PLASMINOGEN ACTIVATION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN ISOLATION; PROTEIN STABILITY; TEMPERATURE SENSITIVITY;

CELL LINE; CRYSTALLOGRAPHY, X-RAY; HEAT; KRINGLES; LIGANDS; MASS SPECTROMETRY; MUTAGENESIS, SITE-DIRECTED; PROTEIN BINDING; PROTEIN FOLDING; RECOMBINANT FUSION PROTEINS; THERMODYNAMICS; TISSUE PLASMINOGEN ACTIVATOR; TRYPTOPHAN;

PICHIA PASTORIS; SACCHAROMYCETALES;

EID: 0030791884     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi970197g     Document Type: Article

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