Real-Time Growth Kinetics Analysis of Macromolecular Assemblies in Cells with Single Molecule Resolution Published as part of The Journal of Physical Chemistry virtual special issue ?Early-Career and Emerging Researchers in Physical Chemistry Volume 2?.

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dc.contributor.authorDanial, John S. H.
dc.contributor.authorJenner, Andreas
dc.contributor.authorGarcia-Saez, Ana J.
dc.contributor.authorCosentino, Katia
dc.date.accessioned2023-07-12T06:55:41Z-
dc.date.available2023-07-12T06:55:41Z-
dc.date.issued2023
dc.identifier.issn1089-5639
dc.identifier.urihttp://osnascholar.ub.uni-osnabrueck.de/handle/unios/71899-
dc.description.abstractSingle molecule fluorescence microscopy has the unique advantage to provide real-time information on the spatiotemporal assembly of individual protein complexes in cellular membranes. This includes the assembly of proteins into oligomer species of numerous copy numbers. However, there is a need for improved tracing analysis of the real-time growth kinetics of these assemblies in cells with single molecule resolution. Here, we present an automated analysis software to accurately measure the real-time kinetics of assembly of individual high-order oligomer complexes. Our software comes with a simple Graphical User Interface (GUI), is available as a source code and an executable, and can analyze a full data set of several hundred to thousand molecules in less than 2 minutes. Importantly, this software is suitable for the analysis of intracellular protein oligomers, whose stoichiometry is usually more difficult to quantify due to variability in signal detection in the different areas of the cell. We validated our method with simulated ground-truth data and time-lapse images of diffraction-limited oligomeric assemblies of BAX and BAK proteins on mitochondria of cells undergoing apoptosis. Our approach provides the broad community of biologists with a fast, user-friendly tool to trace the compositional evolution of macromolecular assemblies, and potentially model their growth for a deeper understanding of the structural and biophysical mechanisms underlying their functions.
dc.description.sponsorshipInternational Max-Planck Research School; University of Tubingen; King's College, University of Cambridge; DFG [SFB944-P26, SFB1557-P5]; ERC; This work was supported by a scholarship from the International Max-Planck Research School and the University of Tubingen awarded to A.J., a research associateship from King's College, University of Cambridge awarded to J.S.H.D., a consolidator (APOSITE) ERC grant awarded to A.J.G.-S., and DFG Grants SFB944-P26 and SFB1557-P5 awarded to K.C.
dc.language.isoen
dc.publisherAMER CHEMICAL SOC
dc.relation.ispartofJOURNAL OF PHYSICAL CHEMISTRY A
dc.subjectChemistry
dc.subjectChemistry, Physical
dc.subjectPhysics
dc.subjectPhysics, Atomic, Molecular & Chemical
dc.subjectPROTEIN
dc.subjectSUPERRESOLUTION MICROSCOPY
dc.titleReal-Time Growth Kinetics Analysis of Macromolecular Assemblies in Cells with Single Molecule Resolution Published as part of The Journal of Physical Chemistry virtual special issue ?Early-Career and Emerging Researchers in Physical Chemistry Volume 2?.
dc.typejournal article
dc.identifier.doi10.1021/acs.jpca.3c00368
dc.identifier.isiISI:000973174300001
dc.contributor.orcidhttp://orcid.org/0000-0002-3796-3500
dc.contributor.researcheridABG-8069-2020
dc.identifier.eissn1520-5215
dc.publisher.place1155 16TH ST, NW, WASHINGTON, DC 20036 USA
dcterms.isPartOf.abbreviationJ. Phys. Chem. A
local.import.remainsaffiliations : University of Cambridge; University of Cambridge; University Osnabruck; University Osnabruck
local.import.remainsearlyaccessdate : APR 2023
local.import.remainsweb-of-science-index : Science Citation Index Expanded (SCI-EXPANDED)
crisitem.author.deptFB 05 - Biologie/Chemie-
crisitem.author.deptidfb05-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.netidCoKa893-
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