Screening of conformationally constrained random polypeptide libraries displayed on a protein scaffold

N. Doi, H. Yanagawa

研究成果: Review article査読

15 被引用数 (Scopus)

抄録

The selection of novel proteins or enzymes from random protein libraries has come to be a major objective in current biology, and these enzymes should prove useful in various biological and biomedical fields. New technologies such as in vitro selection of proteins in cell-free systems have high potential to realize evolutionary molecular engineering of proteins. This review highlights an application of insertional mutagenesis of proteins to evolutionary molecular engineering. Random sequence proteins are inserted into the surface of a host enzyme which serves as a scaffold to display random protein libraries. Constraints on random polypeptide conformations owing to the proximity of N- and C-termini on the scaffold would result in greater screening efficiency of libraries. The scaffold enzyme is also used as a probe for monitoring the hill climbing of random sequence proteins on a fitness landscape and navigating rapid protein folding in the sequence space.

本文言語English
ページ(範囲)394-404
ページ数11
ジャーナルCellular and Molecular Life Sciences
54
5
DOI
出版ステータスPublished - 1998 6月 18
外部発表はい

ASJC Scopus subject areas

  • 分子医療
  • 分子生物学
  • 薬理学
  • 細胞および分子神経科学
  • 細胞生物学

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