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Fast-folding proteins under stress

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Abstract

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 high-temperature 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.

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Acknowledgments

This work was supported by grants from the NSF (MCB 1413256) and from the NIH (2R01 GM093318). The authors wish to thank Dr. Shahar Sukenik for a critical reading and helpful comments on the manuscript.

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  1. Center for Biophysics and Quantitative Biology, University of Illinois at Urbana-Champaign, Urbana, IL, 61801, USA

    Kapil Dave & Martin Gruebele

  2. Departments of Chemistry and Physics, University of Illinois at Urbana-Champaign, Urbana, IL, 61801, USA

    Martin Gruebele

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Dave, K., Gruebele, M. Fast-folding proteins under stress. Cell. Mol. Life Sci. 72, 4273–4285 (2015). https://doi.org/10.1007/s00018-015-2002-3

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