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Analytical biochemistry

Weighing up protein folding

Nature volume 468, pages 640–641 (2010)Cite this article

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Labelling molecules by fast oxidation allows mass spectrometry to study protein folding at submillisecond time resolution. The method also brings a wealth of structural information about protein folding within reach.

When it comes to protein-folding studies, mass spectrometry can provide much structural information. But its time resolution has been insufficient to detect the fastest folding events, which occur on the microsecond timescale1. Chen et al.2 now report a solution to this problem in their study of the submillisecond folding of the barstar protein, published in the Journal of the American Chemical Society. They have married two techniques that could potentially reach microsecond resolution: laser temperature jumping (T-jumping), which initiates protein-folding reactions, and fast photochemical oxidation of the protein (FPOP), which allows mass spectrometry to monitor how far folding has progressed. Their technique should enable more structural information to be obtained from studies of protein-folding kinetics — crucial for developing the next generation of computational methods for simulating protein dynamics, and to allow more complex proteins and protein complexes to be studied experimentally.

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Figure 1: Improving the time resolution of mass spectrometry in protein-folding studies.

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Authors and Affiliations

  1. Martin Gruebele is in the Departments of Chemistry and of Physics, the Center for Biophysics and Computational Biology, and at the Beckman Institute, University of Illinois, 600 South Mathews Avenue, Urbana, Illinois 61801, USA. mgruebel@illinois.edu,

    Martin Gruebele

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  1. Martin Gruebele
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Gruebele, M. Weighing up protein folding. Nature 468, 640–641 (2010). https://doi.org/10.1038/468640a

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