Data on the peptide mapping and MS identification for phosphorylated peptide

Hui Wang; Zong-Cai Tu; Guang-Xian Liu; Lu Zhang; Yuan Chen

doi:10.1016/j.dib.2016.05.009

Data on the peptide mapping and MS identification for phosphorylated peptide

Data Brief. 2016 May 12:8:26-30. doi: 10.1016/j.dib.2016.05.009. eCollection 2016 Sep.

Authors

Hui Wang¹, Zong-Cai Tu², Guang-Xian Liu³, Lu Zhang³, Yuan Chen³

Affiliations

¹ State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang, Jiangxi, China.
² State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang, Jiangxi, China; College of Life Sciences, Jiangxi Normal University, Nanchang, Jiangxi, China.
³ College of Life Sciences, Jiangxi Normal University, Nanchang, Jiangxi, China.

Abstract

This article contains peptides mapping, mass spectrometry and processed data related to the research "Identification and quantification of the phosphorylated ovalbumin by high resolution mass spectrometry under dry-heating treatment" [1]. Fourier transform ion cyclotron mass spectrometry (FTICR MS) was used to investigate the specific phosphorylation sites and the degree of phosphorylation (DSP) at each site. Specifically, phosphorylated peptides were monitored through mass shift on the FTICR MS spectrum. DSP was evaluated through the relative abundance levels of the FTICR MS spectrometry. From these data, the calculation method of DSP was exemplified.