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Quantitative mass imaging of single biological macromolecules.
Young, Gavin; Hundt, Nikolas; Cole, Daniel; Fineberg, Adam; Andrecka, Joanna; Tyler, Andrew; Olerinyova, Anna; Ansari, Ayla; Marklund, Erik G; Collier, Miranda P; Chandler, Shane A; Tkachenko, Olga; Allen, Joel; Crispin, Max; Billington, Neil; Takagi, Yasuharu; Sellers, James R; Eichmann, Cédric; Selenko, Philipp; Frey, Lukas; Riek, Roland; Galpin, Martin R; Struwe, Weston B; Benesch, Justin L P; Kukura, Philipp.
Afiliación
  • Young G; Physical and Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, South Parks Road, Oxford OX1 3QZ, UK.
  • Hundt N; Physical and Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, South Parks Road, Oxford OX1 3QZ, UK.
  • Cole D; Physical and Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, South Parks Road, Oxford OX1 3QZ, UK.
  • Fineberg A; Physical and Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, South Parks Road, Oxford OX1 3QZ, UK.
  • Andrecka J; Physical and Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, South Parks Road, Oxford OX1 3QZ, UK.
  • Tyler A; Physical and Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, South Parks Road, Oxford OX1 3QZ, UK.
  • Olerinyova A; Physical and Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, South Parks Road, Oxford OX1 3QZ, UK.
  • Ansari A; Physical and Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, South Parks Road, Oxford OX1 3QZ, UK.
  • Marklund EG; Department of Chemistry Biomedicinskt Centrum, Uppsala University, Box 576, 75123 Uppsala, Sweden.
  • Collier MP; Physical and Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, South Parks Road, Oxford OX1 3QZ, UK.
  • Chandler SA; Physical and Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, South Parks Road, Oxford OX1 3QZ, UK.
  • Tkachenko O; Physical and Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, South Parks Road, Oxford OX1 3QZ, UK.
  • Allen J; Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, Oxford OX1 3QU, UK.
  • Crispin M; Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, Oxford OX1 3QU, UK.
  • Billington N; Cell Biology and Physiology Center, National Heart, Lung and Blood Institute (NHLBI), Bethesda, MD 20892, USA.
  • Takagi Y; Cell Biology and Physiology Center, National Heart, Lung and Blood Institute (NHLBI), Bethesda, MD 20892, USA.
  • Sellers JR; Cell Biology and Physiology Center, National Heart, Lung and Blood Institute (NHLBI), Bethesda, MD 20892, USA.
  • Eichmann C; In-Cell NMR Laboratory, Department of NMR-supported Structural Biology, Leibniz Institute of Molecular Pharmacology (FMP Berlin), Robert-Rössle Straße 10, 13125 Berlin, Germany.
  • Selenko P; In-Cell NMR Laboratory, Department of NMR-supported Structural Biology, Leibniz Institute of Molecular Pharmacology (FMP Berlin), Robert-Rössle Straße 10, 13125 Berlin, Germany.
  • Frey L; Laboratory of Physical Chemistry, Department of Chemistry and Applied Biosciences, ETH Zürich, 8093 Zürich, Switzerland.
  • Riek R; Laboratory of Physical Chemistry, Department of Chemistry and Applied Biosciences, ETH Zürich, 8093 Zürich, Switzerland.
  • Galpin MR; Department of Immunology and Microbiology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
  • Struwe WB; Physical and Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, South Parks Road, Oxford OX1 3QZ, UK.
  • Benesch JLP; Physical and Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, South Parks Road, Oxford OX1 3QZ, UK.
  • Kukura P; Physical and Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, South Parks Road, Oxford OX1 3QZ, UK. justin.benesch@chem.ox.ac.uk philipp.kukura@chem.ox.ac.uk.
Science ; 360(6387): 423-427, 2018 04 27.
Article en En | MEDLINE | ID: mdl-29700264
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.
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Texto completo: 1 Banco de datos: MEDLINE Asunto principal: Proteínas / Polimerizacion / Agregación Patológica de Proteínas / Imagen Individual de Molécula / Microscopía de Interferencia Límite: Humans Idioma: En Revista: Science Año: 2018 Tipo del documento: Article País de afiliación: Reino Unido
Texto completo
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Texto completo: 1 Banco de datos: MEDLINE Asunto principal: Proteínas / Polimerizacion / Agregación Patológica de Proteínas / Imagen Individual de Molécula / Microscopía de Interferencia Límite: Humans Idioma: En Revista: Science Año: 2018 Tipo del documento: Article País de afiliación: Reino Unido