Partial acetylation of lysine residues improves intraprotein cross-linking

作者: Xin Guo , Pradipta Bandyopadhyay , Birgit Schilling , Malin M Young , Naoaki Fujii

DOI: 10.1021/AC701636W

关键词: Cytochrome cChemistryLysineAmino acidDenaturation (biochemistry)CytochromeBromodomainAcetylationBiochemistryProtein structure

摘要: Intramolecular cross-linking coupled with mass spectrometric identification of cross-linked amino acids is a rapid method for elucidating low-resolution protein tertiary structures or fold families. However, previous studies on model proteins, such as cytochrome c and ribonuclease A, identified limited number peptide cross-links that are biased toward only few the potentially reactive lysine residues. Here, we report an approach to improve diversity intramolecular starting systematic quantitation reactivity residues protein, bovine c. Relative reactivities among 18 were determined by ratio d0 acetyl-d3 groups at each after partial acetylation sulfosuccinimidyl acetate followed denaturation quantitative remaining unmodified lysines acetic-d6 anhydride. These then compared theoretically de...

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