Structural Proteins Analysis of Phage pEp_SNUABM_08

Mass spectrometric analysis of the structural proteins of phage pEp_SNUABM_08 was performed as described [23 (link)]. The phage proteins prepared by implementing five rounds of freeze–thaw cycles were separated using 12% SDS-PAGE. Subsequently, the proteins spanning the entire lane were in-gel digested with trypsin (100 ng/μL). The resultant proteins derived from pEp_SNUABM_08 were identified by using a nano high-resolution LC-MS/MS spectrometer Q Exactive Hybrid Quadrupole-Orbitrap (Thermo Scientific, MA, USA) equipped with the Dionex U 3000 RSLC nano HPLC system.

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Kim S.G., Roh E., Park J., Giri S.S., Kwon J., Kim S.W., Kang J.W., Lee S.B., Jung W.J., Lee Y.M., Cho K, & Park S.C. (2021). The Bacteriophage pEp_SNUABM_08 Is a Novel Singleton Siphovirus with High Host Specificity for Erwinia pyrifoliae. Viruses, 13(7), 1231.

Publication 2021

Q Exactive Hybrid Quadrupole-Orbitrap Dionex U 3000 RSLC nano HPLC system

Freeze Hplc Hybrid Mass spectrometric Ms ms Phage Proteins Sds page Trypsin

Corresponding Organization : Seoul National University

Other organizations : Rural Development Administration

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Variable analysis

independent variables

Freeze–thaw cycles for protein preparation

dependent variables

Structural proteins of phage pEp_SNUABM_08 identified by nano high-resolution LC-MS/MS

control variables

SDS-PAGE for protein separation
Trypsin digestion (100 ng/μL) for in-gel protein digestion
Dionex U 3000 RSLC nano HPLC system for liquid chromatography
Q Exactive Hybrid Quadrupole-Orbitrap (Thermo Scientific, MA, USA) for mass spectrometry

controls

No positive or negative controls were explicitly mentioned in the provided information.

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