Tyrosine deprotonation yields abundant and selective backbone cleavage in peptide anions upon negative electron transfer dissociation and ultraviolet photodissociation.
Tyrosine deprotonation yields abundant and selective backbone cleavage in peptide anions upon negative electron transfer dissociation and ultraviolet photodissociation.
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DOI:
10.1021/ja3032086
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发表时间:
2012-09-26
影响因子:
15
通讯作者:
Brodbelt, Jennifer S.
中科院分区:
文献类型:
--
作者:
Shaw, Jared B.;Ledvina, Aaron R.;Zhang, Xing;Julian, Ryan R.;Brodbelt, Jennifer S.
Tyrosine deprotonation in peptides yields preferential electron detachment upon NETD or UVPD, resulting in prominent N – Cα bond cleavage N-terminal to the tyrosine residue. UVPD of iodo-tyrosine modified peptides was used to generate localized radicals on neutral tyrosine side chains by homolytic cleavage of the C – I bond. Subsequent collisional activation of the radical species yielded the same preferential cleavage of the adjacent N-terminal N – Cα bond. LC-MS/MS analysis of a tryptic digest of BSA demonstrated that these cleavages are regularly observed for peptides when using high pH mobile phases.
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