Physical and molecular bases of protein thermal stability and cold adaptation

Curr Opin Struct Biol. 2017 Feb:42:117-128. doi: 10.1016/j.sbi.2016.12.007. Epub 2016 Dec 29.

Abstract

The molecular bases of thermal and cold stability and adaptation, which allow proteins to remain folded and functional in the temperature ranges in which their host organisms live and grow, are still only partially elucidated. Indeed, both experimental and computational studies fail to yield a fully precise and global physical picture, essentially because all effects are context-dependent and thus quite intricate to unravel. We present a snapshot of the current state of knowledge of this highly complex and challenging issue, whose resolution would enable large-scale rational protein design.

Publication types

  • Review
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adaptation, Physiological*
  • Biophysical Phenomena*
  • Cold Temperature*
  • Humans
  • Ligands
  • Protein Stability
  • Proteins / chemistry*
  • Proteins / metabolism*

Substances

  • Ligands
  • Proteins