抄録
Random sequences of 120-130 amino acid residues were inserted into a surface loop region of Escherichia coli RNase HI. This library was screened and about 10% of the clones were found to retain RNase H activity. Subsequent random mutagenesis led to an increase in RNase H activity and solubility of the protein. The inserted regions mere found not to contribute to the secondary structure of the mutant protein. The high frequency of insertion of flexible sequences and the increase in the protein's function by further mutagenesis simulate one of the events in protein evolution.
本文言語 | English |
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ページ(範囲) | 177-180 |
ページ数 | 4 |
ジャーナル | FEBS Letters |
巻 | 402 |
号 | 2-3 |
DOI | |
出版ステータス | Published - 1997 1月 27 |
外部発表 | はい |
ASJC Scopus subject areas
- 生物理学
- 構造生物学
- 生化学
- 分子生物学
- 遺伝学
- 細胞生物学