Effects of metal binding affinity on the chemical and thermal stability of site-directed mutants of rat oncomodulin

Biophysical Chemistry

Volumn 71, Issue 2-3, 1998, Pages 157-172

  Zheng, Lili ^a   Hogue, Christopher W v ^b   Brennan, John D ^a  

^a BROCK UNIVERSITY   (Canada)

^b MOUNT SINAI HOSPITAL   (Canada)

Author keywords

Fluorescence; Oncomodulin; Protein; Stability; Tryptophan

Indexed keywords

CALCIUM; MAGNESIUM; ONCOMODULIN; TRYPTOPHAN;

ANIMAL CELL; ANIMAL TISSUE; ARTICLE; BINDING AFFINITY; BINDING SITE; GENETIC ENGINEERING; HYDROGEN BOND; METAL BINDING; NONHUMAN; PRIORITY JOURNAL; PROTEIN DENATURATION; RAT; SITE DIRECTED MUTAGENESIS; THERMOSTABILITY;

ACRYLAMIDE; ACRYLAMIDES; ANIMALS; CALCIUM; CALCIUM-BINDING PROTEINS; FLUORESCENCE; GUANIDINE; HYDROGEN BONDING; METALS; MUTAGENESIS, SITE-DIRECTED; MUTATION; NEOPLASM PROTEINS; PROTEIN BINDING; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; RATS; TEMPERATURE; TERBIUM; THERMODYNAMICS; TRYPTOPHAN;

ANIMALIA;

EID: 0032550194     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0301-4622(98)00096-9     Document Type: Article

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