Substitution of aspartic acid with glutamic acid increases the unfolding transition temperature of a protein

Biochemical and Biophysical Research Communications

Volumn 320, Issue 3, 2004, Pages 900-906

  Lee, Duck Yeon ^a   Kim, Kyeong Ae ^a   Yu, Yeon Gyu ^a   Kim, Key Sun ^a  

^a Korea Institute of Science and Technology   (South Korea)

Author keywords

Aspartic acid; Glutamic acid; Protein stability; Thermophile protein

Indexed keywords

ASPARTIC ACID; GLUTAMIC ACID; PROTEIN; THIOREDOXIN;

AMINO ACID ANALYSIS; AMINO ACID SUBSTITUTION; ARTICLE; ENERGY; ESCHERICHIA COLI; METHANOCOCCUS JANNASCHII; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FOLDING; PROTEIN STABILITY; TEMPERATURE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ASPARTIC ACID; BACTERIAL PROTEINS; COMPUTER SIMULATION; EURYARCHAEOTA; GLUTAMIC ACID; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; MUTATION; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; RECOMBINANT PROTEINS; SPECIES SPECIFICITY; STRUCTURE-ACTIVITY RELATIONSHIP; THIOREDOXIN; TRANSITION TEMPERATURE;

EID: 3042796482     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.06.031     Document Type: Article

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