Ontology highlight
ABSTRACT:
SUBMITTER: Shaw JB
PROVIDER: S-EPMC3459303 | biostudies-literature | 2012 Sep
REPOSITORIES: biostudies-literature
Shaw Jared B JB Ledvina Aaron R AR Zhang Xing X Julian Ryan R RR Brodbelt Jennifer S JS
Journal of the American Chemical Society 20120914 38
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 BS ...[more]