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Main Title: Noncovalently associated peptides observed during liquid chromatography-mass spectrometry and their effect on cross-link analyses
Author(s): Giese, Sven H.
Belsom, Adam
Sinn, Ludwig
Fischer, Lutz
Rappsilber, Juri
Type: Article
Abstract: Cross-linking mass spectrometry draws structural information from covalently linked peptide pairs. When these links do not match to previous structural models, they may indicate changes in protein conformation. Unfortunately, such links can also be the result of experimental error or artifacts. Here, we describe the observation of noncovalently associated peptides during liquid chromatography-mass spectrometry analysis, which can easily be misidentified as cross-linked. Strikingly, they often mismatch to the protein structure. Noncovalently associated peptides presumably form during ionization and can be distinguished from cross-linked peptides by observing coelution of the corresponding linear peptides in MS1 spectra, as well as the presence of the individual (intact) peptide fragments in MS2 spectra. To suppress noncovalent peptide formations, increasingly disruptive ionization settings can be used, such as in-source fragmentation.
Subject(s): proteomics
Issue Date: 16-Jan-2019
Date Available: 11-Mar-2021
Is Part Of: 10.14279/depositonce-12031
Language Code: en
DDC Class: 570 Biowissenschaften; Biologie
Sponsor/Funder: DFG, 25065445, SFB 740: Von Molekülen zu Modulen: Organisation und Dynamik zellulärer Funktionseinheiten
Journal Title: Analytical Chemistry
Publisher: American Chemical Society (ACS)
Volume: 91
Issue: 4
Publisher DOI: 10.1021/acs.analchem.8b04037
Page Start: 2678
Page End: 2685
EISSN: 1520-6882
ISSN: 0003-2700
TU Affiliation(s): Fak. 3 Prozesswissenschaften » Inst. Biotechnologie » FG Bioanalytik
Appears in Collections:Technische Universität Berlin » Publications

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