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Weighing-up protein dynamics: the combination of native mass spectrometry and molecular dynamics simulations
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Biochemistry.ORCID iD: 0000-0002-9804-5009
Univ Oxford, Dept Chem, Chem Res Lab, Mansfield Rd, Oxford OX1 3TA, England.
2019 (English)In: Current opinion in structural biology, ISSN 0959-440X, E-ISSN 1879-033X, Vol. 54, p. 50-58Article, review/survey (Refereed) Published
Abstract [en]

Structural dynamics underpin biological function at the molecular level, yet many biophysical and structural biology approaches give only a static or averaged view of proteins. Native mass spectrometry yields spectra of the many states and interactions in the structural ensemble, but its spatial resolution is limited. Conversely, molecular dynamics simulations are innately high-resolution, but have a limited capacity for exploring all structural possibilities. The two techniques hence differ fundamentally in the information they provide, returning data that reflect different length scales and time scales, making them natural bedfellows. Here we discuss how the combination of native mass spectrometry with molecular dynamics simulations is enabling unprecedented insights into a range of biological questions by interrogating the motions of proteins, their assemblies, and interactions.

Place, publisher, year, edition, pages
CURRENT BIOLOGY LTD , 2019. Vol. 54, p. 50-58
National Category
Structural Biology
Identifiers
URN: urn:nbn:se:uu:diva-390345DOI: 10.1016/j.sbi.2018.12.011ISI: 000473554100008PubMedID: 30743182OAI: oai:DiVA.org:uu-390345DiVA, id: diva2:1341468
Funder
Swedish Research CouncilEU, Horizon 2020Available from: 2019-08-08 Created: 2019-08-08 Last updated: 2019-08-08Bibliographically approved

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