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Milestone 19

Dynamic protein structures

Nature Methods volume 12, page 18 (2015)Cite this article

The native state of most proteins in a cell is a well-defined three-dimensional structure, which is maintained by intramolecular interactions. Detailed knowledge of protein structure allows researchers to determine the molecules' functions and to design inhibitors for medical or research purposes. The traditional methods that are used to elucidate structure, such as X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy, require a lot of time and a large quantity of protein, and, in many cases, the experiments are not successful. In the early 1990s, researchers began to explore how mass spectrometry—a rapid technique that requires only small sample amounts—could be used to provide detailed, dynamic structural information about proteins.

In 1991, several groups began to apply electrospray ionization mass spectrometry (ESI-MS; Milestone 15) to analyze the intact, native structures of protein systems. This approach, now known as native mass spectrometry, allowed the groups to examine the conformational changes that occur within proteins during the unfolding process triggered by harsh conditions.

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References

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Authors and Affiliations

  1. Senior Editor, Nature Communications,

    Rebecca Kirk

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  1. Rebecca Kirk
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Kirk, R. Dynamic protein structures. Nat Methods 12 (Suppl 1), 18 (2015). https://doi.org/10.1038/nmeth.3522

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