Stabilization of Escherichia coli ribonuclease HI by strategic replacement of amino acid residues with those from the thermophilic counterpart

Journal of Biological Chemistry

Volumn 267, Issue 30, 1992, Pages 21535-21542

  Kimura, S ^a   Nakamura, H ^a   Hashimoto, T ^a   Oobatake, M ^a   Kanaya, S ^a  

^a BIOMOL ENG RESEARCH INSTITUTE   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

RIBONUCLEASE H;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME STABILITY; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; THERMOPHILIC BACTERIUM; THERMOSTABILITY; THERMUS THERMOPHILUS;

AMINO ACID SEQUENCE; AMINO ACIDS; BASE SEQUENCE; CIRCULAR DICHROISM; DNA, SINGLE-STRANDED; ENZYME STABILITY; ESCHERICHIA COLI; HEAT; MOLECULAR SEQUENCE DATA; MUTAGENESIS; PLASMIDS; PROTEIN DENATURATION; PROTEIN FOLDING; RIBONUCLEASE H, CALF THYMUS; SEQUENCE ALIGNMENT; THERMUS THERMOPHILUS;

ESCHERICHIA COLI; ITAYA; THERMUS THERMOPHILUS;

EID: 0026803109     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (0)