Glycine-15 in the bend between two α-helices can explain the thermostability of DNA binding protein HU from Bacillus stearothermophilus

Biochemistry

Volumn 35, Issue 4, 1996, Pages 1195-1200

  Kawamura, Shunsuke ^a   Kakuta, Yoshimitsu ^b   Tanaka, Isao ^b   Hikichi, Kunio ^b   Kuhara, Satoru ^a   Yamasaki, Nobuyuki ^a   Kimura, Makoto ^a  

^a KYUSHU UNIVERSITY   (Japan)

^b HOKKAIDO UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; DNA BINDING PROTEIN; GLYCINE; HYDROGEN; MUTANT PROTEIN;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; CIRCULAR DICHROISM; GEOBACILLUS STEAROTHERMOPHILUS; HYDROGEN BOND; MUTANT; NONHUMAN; PRIORITY JOURNAL; PROTEIN STABILITY; PROTON NUCLEAR MAGNETIC RESONANCE; THERMOSTABILITY;

BACILLUS STEAROTHERMOPHILUS; BACTERIAL PROTEINS; BASE SEQUENCE; DNA-BINDING PROTEINS; GENES, BACTERIAL; GLYCINE; HEAT; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PROTEIN DENATURATION; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS;

BACILLUS SUBTILIS; GEOBACILLUS STEAROTHERMOPHILUS;

EID: 0029670677     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi951581l     Document Type: Article

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