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Journal of Biological Chemistry

Volumn 275, Issue 35, 2000, Pages 27129-27136

The stabilities of mammalian apomyoglobins vary over a 600-fold range and can be enhanced by comparative mutagenesis

(3) Scott, Emily E a Paster, Eden V a Olson, John S a

a RICE UNIVERSITY (United States)

Author keywords

[No Author keywords available]

Indexed keywords

APOMYOGLOBIN; RECOMBINANT PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; CONTROLLED STUDY; HUMAN; MAMMAL; MUTAGENESIS; NONHUMAN; OXYGEN AFFINITY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DENATURATION; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN STABILITY; SEQUENCE HOMOLOGY; SPECIES DIFFERENCE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMALS; APOPROTEINS; CIRCULAR DICHROISM; MAMMALS; MOLECULAR SEQUENCE DATA; MUTAGENESIS; MYOGLOBIN; PROTEIN CONFORMATION; PROTEIN FOLDING; SEQUENCE HOMOLOGY, AMINO ACID; SPECIES SPECIFICITY; SPECTROMETRY, FLUORESCENCE;

CETACEA; EQUUS CABALLUS; MAMMALIA; OVIS ARIES; PHYSETER CATODON; PHYSETERIDAE; SUS SCROFA;

EID: 0034282637 PISSN: 00219258 EISSN: None Source Type: Journal
DOI: 10.1074/jbc.M000452200 Document Type: Article

Times cited : (48)

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