Please use this identifier to cite or link to this item:
Type: Artigo de periódico
Title: Analysis of secondary structure in proteins by chemical cross-linking coupled to MS
Author: Fioramonte, M
dos Santos, AM
McIlwain, S
Noble, WS
Franchini, KG
Gozzo, FC
Abstract: Chemical cross-linking is an attractive technique for the study of the structure of protein complexes due to its low sample consumption and short analysis time. Furthermore, distance constraints obtained from the identification of cross-linked peptides by MS can be used to construct and validate protein models. If a sufficient number of distance constraints are obtained, then determining the secondary structure of a protein can allow inference of the protein's fold. In this work, we show how the distance constraints obtained from cross-linking experiments can identify secondary structures within the protein sequence. Molecular modeling of alpha helices and beta sheets reveals that each secondary structure presents different cross-linking possibilities due to the topological distances between reactive residues. Cross-linking experiments performed with amine reactive cross-linkers with model alpha helix containing proteins corroborated the molecular modeling predictions. The cross-linking patterns established here can be extended to other cross-linkers with known lengths for the determination of secondary structures in proteins.
Subject: Alpha helix
Beta sheet
Protein secondary structure
Country: EUA
Editor: Wiley-blackwell
Rights: fechado
Identifier DOI: 10.1002/pmic.201200040
Date Issue: 2012
Appears in Collections:Unicamp - Artigos e Outros Documentos

Files in This Item:
File Description SizeFormat 
WOS000308098700016.pdf832.04 kBAdobe PDFView/Open

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.