English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Proteome-Wide Structural Probing of Low-Abundant Protein Interactions by Cross-Linking Mass Spectrometry

Fürsch, J., Kammer, K.-M., Kreft, S. G., Beck, M., & Stengel, F. (2020). Proteome-Wide Structural Probing of Low-Abundant Protein Interactions by Cross-Linking Mass Spectrometry. Analytical Chemistry, 92(5), 4016-4022. doi:10.1021/acs.analchem.9b05559.

Item is

Basic

show hide
Genre: Journal Article

Files

show Files

Locators

show

Creators

show
hide
 Creators:
Fürsch, Julius1, Author
Kammer, Kai-Michael1, Author
Kreft, Stefan G.2, Author
Beck, Martin3, 4, Author              
Stengel, Florian1, Author
Affiliations:
1Department of Biology and Konstanz Research School Chemical Biology, University of Konstanz, Konstanz, Germany, ou_persistent22              
2Department of Biology, University of Konstanz, Konstanz, Germany, ou_persistent22              
3Department of Molecular Sociology, Max Planck Institute of Biophysics, Max Planck Society, ou_3040395              
4European Molecular Biology Laboratory, Heidelberg, Germany, ou_persistent22              

Content

show
hide
Free keywords: -
 Abstract: Proteome-wide cross-linking studies have spurred great interest as they facilitate structural probing of protein interactions in living cells and organisms. However, current studies have a bias for high-abundant proteins. In this study we demonstrate both experimentally and by a kinetic model that this bias is also caused by the propensity of cross-links to preferentially form on high abundant proteins and not by the inability to detect cross-links due to limitations in current technology. We further show, by using both an in vitro mimic of a crowded cellular environment and eukaryotic cell lysates, that parameters optimized toward a pseudo first order kinetics model result in a significant increase in the detection of lower-abundant proteins on a proteome-wide scale. Our study therefore explains the cause of a major limitation in current proteome-wide cross-linking studies and demonstrates how to address a larger part of the proteome by cross-linking.

Details

show
hide
Language(s): eng - English
 Dates: 2019-02-032020-02-032020-02-03
 Publication Status: Published online
 Pages: 7
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1021/acs.analchem.9b05559
BibTex Citekey: fursch_proteome-wide_2020
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Analytical Chemistry
  Abbreviation : Anal. Chem.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Washington, D.C. : American Chemical Society
Pages: - Volume / Issue: 92 (5) Sequence Number: - Start / End Page: 4016 - 4022 Identifier: ISSN: 0003-2700
CoNE: https://pure.mpg.de/cone/journals/resource/111032812862552