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Structural biology

Proteins flex to function

Nature volume 438, pages 36–37 (2005)Cite this article

Static pictures of protein structures are so prevalent that it is easy to forget they are dynamic molecular machines. Characterizing their intrinsic motions may be necessary to understand how they work.

Enzymes are proteins that catalyse chemical processes by lowering the energy barriers between substrate and product, thus increasing the rate of reaction. They function by stabilizing transition states, the structural intermediates formed in the rate-limiting steps of chemical reactions. In some cases, the cataly-sis process involves the enzyme interconverting between alternative versions of its structure, which can be followed using nuclear magnetic resonance (NMR) spectroscopy1,2,3. On page 117 of this issue, Eisenmesser et al.4 demonstrate that the slow structural motions between sub-states of an enzyme that take place during catalysis also occur in the free enzyme in the absence of its substrate. This implies that enzymes have a set of pre-existing dynamics, or ‘intrinsic plasticity’, that can determine their function.

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Figure 1: The purpose of plasticity.

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Authors and Affiliations

  1. the Center for Advanced Biotechnology and Medicine, Rutgers University and Robert Wood Johnson Medical School, Piscataway, 08854, New Jersey, USA

    Yuanpeng J. Huang & Gaetano T. Montelione

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  1. Yuanpeng J. Huang
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  2. Gaetano T. Montelione
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Huang, Y., Montelione, G. Proteins flex to function. Nature 438, 36–37 (2005). https://doi.org/10.1038/438036a

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