Analysis of Metal-binding Proteins by Mass Spectrometry

2016 Fiscal Year Final Research Report

• Project/Area Number: 26505016
• Research Category: Grant-in-Aid for Scientific Research (C)
• Allocation Type: Multi-year Fund
• Section: 一般
• Research Field: オミクス計測科学
• Research Institution: National Institute of Advanced Industrial Science and Technology (2015-2016); The Institute of Physical and Chemical Research (2014)
• Principal Investigator: Asakawa Daiki 国立研究開発法人産業技術総合研究所, 分析計測標準研究部門, 主任研究員 (60584365)
• Project Period (FY): 2014-04-01 – 2017-03-31
• Keywords: Analytical Chemistry / Mass Spectrometry

Outline of Final Research Achievements

Electn transfer dissociation (ETD) tandem mass spectrometry have been used as analytical method for characterization of protein. Since ECD/ETD involved the recombination between peptide ion and electron/anion, employing ions with a higher charge state as the precursor dramatically increases the yield of radical reactive species and thereby improving the sequence coverage obtained with ETD. Hoerver, the charge state of peptides is dependent on the peptide sequence, especially on the number of basic residues. For analysis of tryptic peptides, the N-terminal amino group and the C-terminal basic residue are protonated, often yielding doubly protonated species. However, double protonation is not enough for the ion/electron reaction of ETD to yield better sequence coverage. We found that the use of a suitable metal salt in analyte solution would increase the charge state of tryptic peptide ions containing acidic residues and provide information useful for sequencing by ETD.

Free Research Field

分析化学、質量分析