Nature Communications (May 2017)

An optimized strategy to measure protein stability highlights differences between cold and hot unfolded states

  • Caterina Alfano,
  • Domenico Sanfelice,
  • Stephen R. Martin,
  • Annalisa Pastore,
  • Piero Andrea Temussi

DOI
https://doi.org/10.1038/ncomms15428
Journal volume & issue
Vol. 8, no. 1
pp. 1 – 9

Abstract

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Crowding effects—important when considering cellular environments—greatly influence protein stability. Here the authors study the impact of macromolecular crowders on high and low temperature protein unfolding, and show that volume exclusion effects are larger when the protein and crowder volumes are similar.