Quantitative mass imaging of single biological macromolecules-Reference-Cited by-同舟云学术

Quantitative mass imaging of single biological macromolecules

Published:2018-04-27 Issue:6387 Volume:360 Page:423-427
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Young Gavin¹^ORCID,Hundt Nikolas¹^ORCID,Cole Daniel¹,Fineberg Adam¹^ORCID,Andrecka Joanna¹,Tyler Andrew¹^ORCID,Olerinyova Anna¹^ORCID,Ansari Ayla¹^ORCID,Marklund Erik G.²^ORCID,Collier Miranda P.¹,Chandler Shane A.¹,Tkachenko Olga¹,Allen Joel³^ORCID,Crispin Max³^ORCID,Billington Neil⁴^ORCID,Takagi Yasuharu⁴,Sellers James R.⁴,Eichmann Cédric⁵,Selenko Philipp⁵,Frey Lukas⁶,Riek Roland⁶⁷,Galpin Martin R.¹^ORCID,Struwe Weston B.¹^ORCID,Benesch Justin L. P.¹^ORCID,Kukura Philipp¹^ORCID

Affiliation:

1. Physical and Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, South Parks Road, Oxford OX1 3QZ, UK.

2. Department of Chemistry Biomedicinskt Centrum, Uppsala University, Box 576, 75123 Uppsala, Sweden.

3. Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, Oxford OX1 3QU, UK.

4. Cell Biology and Physiology Center, National Heart, Lung and Blood Institute (NHLBI), Bethesda, MD 20892, USA.

5. In-Cell NMR Laboratory, Department of NMR-supported Structural Biology, Leibniz Institute of Molecular Pharmacology (FMP Berlin), Robert-Rössle Straße 10, 13125 Berlin, Germany.

6. Laboratory of Physical Chemistry, Department of Chemistry and Applied Biosciences, ETH Zürich, 8093 Zürich, Switzerland.

7. Department of Immunology and Microbiology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.

Abstract

Watching proteins' weight Careful measurements of light scattering can provide information on individual macromolecules and complexes. Young et al. used a light-scattering approach for accurate mass determination of proteins as small as 20 kDa (see the Perspective by Lee and Klenerman). Movies of protein complex association and dissociation were analyzed to extract biophysical parameters from single molecules and assemblies without labeling. Using this approach, the authors determined in vitro kinetics of fibril and aggregate growth and association constants for a complex protein-glycoprotein assembly. Science , this issue p. 423 ; see also p. 378

Funder

FP7 People: Marie-Curie Actions

Engineering and Physical Sciences Research Council

Biotechnology and Biological Sciences Research Council

European Research Council

Swiss National Science Foundation

Deutsche Forschungsgemeinschaft

Center for HIV/AIDS Vaccine Immunology and Immunogen Discovery

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary