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Quantitative mass imaging of single biological macromolecules.

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Title: Quantitative mass imaging of single biological macromolecules.
Authors: Young, Gavin (AUTHOR), Hundt, Nikolas (AUTHOR), Cole, Daniel (AUTHOR), Fineberg, Adam (AUTHOR), Andrecka, Joanna (AUTHOR), Tyler, Andrew (AUTHOR), Olerinyova, Anna (AUTHOR), Ansari, Ayla (AUTHOR), Marklund, Erik G. (AUTHOR), Collier, Miranda P. (AUTHOR), Chandler, Shane A. (AUTHOR), Tkachenko, Olga (AUTHOR), Allen, Joel (AUTHOR), Crispin, Max (AUTHOR), Billington, Neil (AUTHOR), Takagi, Yasuharu (AUTHOR), Sellers, James R. (AUTHOR), Eichmann, Cédric (AUTHOR), Selenko, Philipp (AUTHOR), Frey, Lukas (AUTHOR)
Source: Science (pre-March 2025). 4/27/2018, Vol. 360 Issue 6387, p423-427. 5p. 1 Diagram, 3 Graphs.
Subjects: Cytology, Proteins, Interferometry, Biomolecules, Molecular dynamics
Abstract: 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 the molecular 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. [ABSTRACT FROM AUTHOR]
Copyright of Science (pre-March 2025) is the property of American Association for the Advancement of Science and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
Database: Psychology and Behavioral Sciences Collection
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  Data: <searchLink fieldCode="JN" term="%22Science+%28pre-March+2025%29%22">Science (pre-March 2025)</searchLink>. 4/27/2018, Vol. 360 Issue 6387, p423-427. 5p. 1 Diagram, 3 Graphs.
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  Data: 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 the molecular 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. [ABSTRACT FROM AUTHOR]
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  Data: <i>Copyright of Science (pre-March 2025) is the property of American Association for the Advancement of Science and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
PLink https://search.ebscohost.com/login.aspx?direct=true&site=eds-live&db=pbh&AN=129326977
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        Value: 10.1126/science.aar5839
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        Text: English
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