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Democratizing the mapping of gene mutations to protein biophysics

A general method that quantifies and disentangles the effects of a gene’s mutations on the traits of its protein enables assessments of mutational effects on protein biophysics for many of the proteins of a living organism.
By
  1. Debora S. Marks

    1. Debora S. Marks is in the Department of Systems Biology, Harvard Medical School, Boston, Massachusetts 02115, USA, and at the Broad Institute of Harvard and MIT, Cambridge, Massachusetts.

  2. Stephen W. Michnick

    1. Stephen W. Michnick is in the Department of Biochemistry, University of Montreal, Montreal H3C 3J7, Canada.

Proteins function through their interactions with other biomolecules, and can be modulated not only by changes to the amino-acid residues at the protein–biomolecule interface, but also by changes at distal sites — a phenomenon called allostery. Discovering which protein sites are allosteric has been difficult, because methods that simply and comprehensively quantify allosteric effects have been lacking. Writing in Nature, Faure et al.1 report the first integrated method to globally map, quantify and distinguish the effects of mutations on allostery and protein stability. Their approach is also easy to do, making it as accessible to geneticists as it is to biophysicists. This method will have broad applications in biotechnology and drug discovery.

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Nature 604, 47-48 (2022)

doi: https://doi.org/10.1038/d41586-022-00870-5

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Competing Interests

The authors declare no competing interests.

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