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Liquid chromatography/tandem mass spectrometry of synthesis products associated with the viral protein U S 11
Author(s) -
Garzotti Marco,
Hamdan Mahmoud
Publication year - 1998
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/(sici)1097-0231(19980715)12:13<843::aid-rcm250>3.0.co;2-w
Subject(s) - chemistry , tandem mass spectrometry , mass spectrometry , chromatography , peptide sequence , electrospray ionization , electrospray , protein mass spectrometry , liquid chromatography–mass spectrometry , amino acid , residue (chemistry) , protein sequencing , tandem mass tag , biochemistry , proteomics , quantitative proteomics , gene
U s 11 is a small basic protein composed of 161 amino acid residues, and is among the most abundant viral proteins in cells infected with herpes simplex viruses HSV1 and HSV2. The amino acid sequence [91–121] is considered essential for the binding of this protein with RNA. Automated solid phase synthesis of this fragment resulted in a crude reaction mixture containing the desired sequence as well as a number of unknown side products. On‐line liquid chromatography/electrospray mass spectrometry (LC/ES‐MS) and LC/ES tandem mass spectrometry (MS/MS) allowed the identification of the separated components and furnished relevant sequencing information. The unusual sequences of the monitored components, which consist of a tandemly repeated three‐amino‐acid motif with the sequence Arg‐X‐Pro, where X is an acidic or uncharged polar amino acid residue, yielded product ion spectra lacking substantial sequence information and rich in fragment ions manifesting the neutral losses 17, 42 and 60 u. © 1998 John Wiley & Sons, Ltd.