Directed evolution to improve protein folding in vivo

Curr Opin Struct Biol. 2018 Feb:48:117-123. doi: 10.1016/j.sbi.2017.12.003. Epub 2017 Dec 23.

Abstract

Recently, several innovative approaches have been developed that allow one to directly screen or select for improved protein folding in the cellular context. These methods have the potential of not just leading to a better understanding of the in vivo folding process, they may also allow for improved production of proteins of biotechnological interest.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Biosensing Techniques / methods*
  • Biotechnology / methods
  • Chaperonin 10 / chemistry*
  • Chaperonin 10 / genetics
  • Chaperonin 10 / metabolism
  • Chaperonin 60 / chemistry*
  • Chaperonin 60 / genetics
  • Chaperonin 60 / metabolism
  • Directed Molecular Evolution / methods*
  • Escherichia coli / genetics
  • Escherichia coli / metabolism
  • Genes, Reporter
  • Green Fluorescent Proteins / genetics
  • Green Fluorescent Proteins / metabolism
  • Kinetics
  • Protein Engineering / methods*
  • Protein Folding
  • Protein Stability
  • Staining and Labeling / methods*
  • Thermodynamics

Substances

  • Chaperonin 10
  • Chaperonin 60
  • Green Fluorescent Proteins