Fast-folding proteins under stress

Kapil Dave, Martin Gruebele

Research output: Contribution to journalReview articlepeer-review


Proteins are subject to a variety of stresses in biological organisms, including pressure and temperature, which are the easiest stresses to simulate by molecular dynamics. We discuss the effect of pressure and thermal stress on very-fast-folding model proteins, whose in vitro folding can be fully simulated on computers and compared with experiments. We then discuss experiments that can be used to subject proteins to low- and higherature unfolding, as well as low- and high-pressure unfolding. Pressure and temperature are prototypical perturbations that illustrate how close many proteins are to instability, a property that cells can exploit to control protein function. We conclude by reviewing some recent in-cell experiments, and progress being made in simulating and measuring protein stability and function inside live cells.

Original languageEnglish (US)
Pages (from-to)4273-4285
Number of pages13
JournalCellular and Molecular Life Sciences
Issue number22
StatePublished - Nov 1 2015


  • Cell cycle
  • Fluorescence
  • Molecular dynamics
  • NTL9
  • Phase diagram
  • Pressure jump
  • Proton NMR
  • Temperature jump
  • WW domain

ASJC Scopus subject areas

  • Molecular Medicine
  • Molecular Biology
  • Pharmacology
  • Cellular and Molecular Neuroscience
  • Cell Biology


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