Unique Fragmentation of Singly Charged DEST Cross-Linked Peptides

被引：8
作者：
He, Yi [1 ]
Lauber, Matthew A. [1 ]
Reilly, James P. [1 ]
机构：
[1] Indiana Univ, Bloomington, IN 47405 USA
来源：
JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY | 2012年 / 23卷 / 06期
基金：
美国国家科学基金会;
关键词：
Cross-linking; Fragmentation pattern; Collisional induced dissociation; MALDI ion trap; MASS-SPECTROMETRIC ANALYSIS; PROTEIN STRUCTURES; STRUCTURAL-ANALYSIS; LINKING REAGENTS; IDENTIFICATION; QUATERNARY; CLEAVAGE; IONS;
D O I：
10.1007/s13361-012-0372-4
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
It has previously been shown that when cross-linking reagent diethyl suberthioimidate (DEST) reacts with primary amines of proteins to yield amidinated residues, the primary amines retain their high basicity, and cross-linked species can be enriched by strong cation exchange. It is now demonstrated that collisional activation of singly-charged DEST cross-linked peptide ions leads to preferential cleavage at the cross-linked sites. The resulting product ions facilitate the detection and identification of cross-linked peptides.
引用
收藏
页码：1046 / 1052
页数：7
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