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Biophysics

May the force be with you

Nature volume 397, pages 20–21 (1999)Cite this article

Many of us grew up with the simplifying assumptions of biology in a test tube — dilute solutions, purified biomolecules and the like. But the biomolecular machinery evolved in a much more complex environment than this. I can remember, several years ago, seeing a cartoon that depicted the remarkably crowded and organized environment of the cytoplasm. I was struck for the first time by the implications of chaperonins for the protein-folding field. It isn’t that the biophysics we learned in the test tube is wrong, or cannot be extrapolated to the living cell, but we must acknowledge that questions of relevance and adequacy sometimes arise.

So too for the field that deals with the molecular details of how proteins and their ligands recognize each other. It is a field dominated by a static viewpoint, where interactions are measured in the test tube and receptor-ligand energetics are characterized by equilibrium thermodynamics. But on page 50 of this issue, Merkel et al.1 report that they have used force measurements on single molecules to show that protein-ligand interaction strengths and dynamics are not fixed in stone. Because the receptor-ligand interaction is governed by thermal activation, the interaction strength and dynamics can be tuned to be weak or strong by varying how fast the retracting force is driven (the ‘loading rate’). Nature is a wonderful engineer and, in cases where variable mechanical loading is biologically relevant2, it might regulate bioadhesive strengths through activation barriers engineered by evolution.

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Figure 1: The streptavidin-biotin receptor-ligand pair.

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  1. The Department of Bioengineering, Box 352125, University of Washington, Seattle, 98195, Washington, USA

    Patrick S. Stayton

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  1. Patrick S. Stayton
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Stayton, P. May the force be with you. Nature 397, 20–21 (1999). https://doi.org/10.1038/16145

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