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Thermostabilization of Escherichia coli ribonuclease HI by replacing left-handed helical Lys95 with Gly or Asn.
Kimura S, Kanaya S, Nakamura H. Kimura S, et al. Among authors: nakamura h. J Biol Chem. 1992 Nov 5;267(31):22014-7. J Biol Chem. 1992. PMID: 1331044 Free article.
From the systematic replacements of amino acid residues of Escherichia coli ribonuclease HI with those of its thermophilic counterpart, the basic protrusion domain including region 6 (R6) from residues 91 to 95 was found to increase the structural stability of the mutant protein …
From the systematic replacements of amino acid residues of Escherichia coli ribonuclease HI with those of its thermophilic counterpart, the …
Cooperative stabilization of Escherichia coli ribonuclease HI by insertion of Gly-80b and Gly-77-->Ala substitution.
Ishikawa K, Nakamura H, Morikawa K, Kimura S, Kanaya S. Ishikawa K, et al. Among authors: nakamura h. Biochemistry. 1993 Jul 20;32(28):7136-42. doi: 10.1021/bi00079a010. Biochemistry. 1993. PMID: 8393706
The insertion of a Gly residue (designated as Gly-80b) between the C-cap of the alpha II-helix (Gln-80) and the N-cap of the alpha III-helix (Trp-81) in Escherichia coli ribonuclease HI enhances the protein stability by 0.4 kcal/mol in delta G (Kimura, S., Nakamura, H …
The insertion of a Gly residue (designated as Gly-80b) between the C-cap of the alpha II-helix (Gln-80) and the N-cap of the alpha III-helix …
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