Ontology highlight
ABSTRACT:
INSTRUMENT(S): LTQ Orbitrap Velos
ORGANISM(S): Escherichia Coli
SUBMITTER: Hao Yang
LAB HEAD: Ping Xu
PROVIDER: PXD008688 | Pride | 2019-01-11
REPOSITORIES: Pride
Yang Hao H Li Yan-Chang YC Zhao Ming-Zhi MZ Wu Fei-Lin FL Wang Xi X Xiao Wei-Di WD Wang Yi-Hao YH Zhang Jun-Ling JL Wang Fu-Qiang FQ Xu Feng F Zeng Wen-Feng WF Overall Christopher M CM He Si-Min SM Chi Hao H Xu Ping P
Molecular & cellular proteomics : MCP 20190108 4
<i>De novo</i> peptide sequencing for large-scale proteomics remains challenging because of the lack of full coverage of ion series in tandem mass spectra. We developed a mirror protease of trypsin, acetylated LysargiNase (Ac-LysargiNase), with superior activity and stability. The mirror spectrum pairs derived from the Ac-LysargiNase and trypsin treated samples can generate full <i>b</i> and <i>y</i> ion series, which provide mutual complementarity of each other, and allow us to develop a novel ...[more]