期刊
SCIENCE
卷 360, 期 6387, 页码 423-+出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aar5839
关键词
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资金
- Zvi and Ofra Meitar Magdalen Graduate Scholarship
- DFG (German Research Foundation) research fellowship [HU 2462/1-1]
- Swedish Research Council
- European Commission for a Marie Sklodowska Curie International Career Grant [2015-00559]
- Oxford University Press
- Biotechnology and Biological Sciences Research Council
- Waters Corp through the iCASE studentship [BB/L017067/1]
- St John's College, University of Oxford
- Engineering and Physical Sciences Research Council (EPSRC) Studentship
- National Institute of Allergy and Infectious Diseases (Center for HIV/AIDS Vaccine Immunology and Immunogen Discovery grant) [UM1AI100663]
- NHLBI intramural program [HL0001786]
- Swiss National Science Foundation advanced postdoctoral mobility fellowship [P300PA160979]
- European Research Council (ERC) Consolidator Grant (NeuroInCellNMR) [647474]
- EPSRC [EP/J01835X/1]
- ERC Starting Investigator Grant (Nanoscope) [337577]
- European Research Council (ERC) [647474] Funding Source: European Research Council (ERC)
- BBSRC [BB/J018082/1] Funding Source: UKRI
- EPSRC [EP/J01835X/1] Funding Source: UKRI
The cellular processes underpinning life are orchestrated by proteins and their interactions. The associated structural and dynamic heterogeneity, despite being key to function, poses a fundamental challenge to existing analytical and structural methodologies. We used interferometric scattering microscopy to quantify the mass of single biomolecules in solution with 2% sequence mass accuracy, up to 19-kilodalton resolution, and 1-kilodalton precision. We resolved oligomeric distributions at high dynamic range, detected small-molecule binding, and mass-imaged proteins with associated lipids and sugars. These capabilities enabled us to characterize themolecular dynamics of processes as diverse as glycoprotein cross-linking, amyloidogenic protein aggregation, and actin polymerization. Interferometric scattering mass spectrometry allows spatiotemporally resolved measurement of a broad range of biomolecular interactions, one molecule at a time.
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