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Structural biology

Protein dynamics from disorder

Nature volume 459, pages 1063–1064 (2009)Cite this article

The functions of proteins are often crucially dependent on how they move, but measuring the absolute magnitudes of protein motions hasn't been possible. A spectroscopic method looks set to change all that.

In the half-century since our first glimpse of a protein structure at atomic resolution, structural biology has had a fundamental role in advancing our understanding of biological function at a molecular level. Yet although it is generally agreed that proteins must have some flexibility in order to perform their roles, uncertainty remains about how well static structural models capture the essential features underlying function. A picture may be worth a thousand words, but does it tell the entire story?

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Figure 1: Molecular alignment enables the detection of protein dynamics.

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  1. Joel R. Tolman is in the Department of Chemistry, Johns Hopkins University, 3400 North Charles Street, Baltimore, Maryland 21218, USA. tolman@jhu.edu,

    Joel R. Tolman

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  1. Joel R. Tolman
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Tolman, J. Protein dynamics from disorder. Nature 459, 1063–1064 (2009). https://doi.org/10.1038/4591063a

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