Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/67131
Type: Artigo de periódico
Title: Fragmentation features of intermolecular cross-linked peptides using N-hydroxy-succinimide esters by MALDI- and ESI-MS/MS for use in structural proteomics
Author: Santos, LFA
Iglesias, AH
Gozzo, FC
Abstract: The use of mass spectrometry coupled with chemical cross-linking of proteins has become one of the most useful tools for proteins structure and interactions studies. One of the challenges in these studies is the identification of the cross-linked peptides. The interpretation of the MS/MS data generated in cross-linking experiments using N-hydroxy succinimide esters is not trivial once a new amide bond is formed allowing new fragmentation pathways, unlike linear peptides. Intermolecular cross-linked peptides occur when two different peptides are connected by the cross-linker and they yield information on the spatial proximity of different domains (within a protein) or proteins (within a complex). In this article, we report a detailed fragmentation study of intermolecular cross-linked peptides, generated from a set of synthetic peptides, using both ESI and MAID! to generate the precursor ions. The fragmentation features observed here can be helpful in the interpretation and identification of cross-linked peptides present in cross-linking experiments and be further implemented in search engine's algorithms. Copyright (C) 2011 John Wiley & Sons, Ltd.
Subject: cross-linking
peptide fragmentation
mass spectrometry
protein structure
MALDI
ESI
Country: EUA
Editor: Wiley-blackwell
Rights: fechado
Identifier DOI: 10.1002/jms.1951
Date Issue: 2011
Appears in Collections:Artigos e Materiais de Revistas Científicas - Unicamp

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