Literature DB >> 6757449

Effect of single amino acid substitutions at the same position on stability of a two-domain protein.

K Yutani, K Ogasahara, A Kimura, Y Sugino.   

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Year:  1982        PMID： 6757449     DOI： 10.1016/0022-2836(82)90184-x

Source DB:  PubMed          Journal:  J Mol Biol        ISSN： 0022-2836            Impact factor:   5.469


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  4 in total

1.  Aspartate transcarbamylase from the deep-sea hyperthermophilic archaeon Pyrococcus abyssi: genetic organization, structure, and expression in Escherichia coli.

Authors:  C Purcarea; G Hervé; M M Ladjimi; R Cunin
Journal:  J Bacteriol       Date:  1997-07       Impact factor: 3.490

2.  Dependence of conformational stability on hydrophobicity of the amino acid residue in a series of variant proteins substituted at a unique position of tryptophan synthase alpha subunit.

Authors:  K Yutani; K Ogasahara; T Tsujita; Y Sugino
Journal:  Proc Natl Acad Sci U S A       Date:  1987-07       Impact factor: 11.205

3.  Isolation of a Bacillus stearothermophilus mutant exhibiting increased thermostability in its restriction endonuclease.

Authors:  J D Hendrix; N E Welker
Journal:  J Bacteriol       Date:  1985-05       Impact factor: 3.490

4.  Isolation of a thermostable enzyme variant by cloning and selection in a thermophile.

Authors:  H Liao; T McKenzie; R Hageman
Journal:  Proc Natl Acad Sci U S A       Date:  1986-02       Impact factor: 11.205
  4 in total

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