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Cyclization of peptide b9 ions
Journal of the American Society for Mass Spectrometry ( IF 3.1 ) Pub Date : 2009 Dec , DOI: 10.1016/j.jasms.2009.08.013
Alex G Harrison 1
Affiliation  

The product ion mass spectra obtained by CID of the b9 ions derived by loss of neutral alanine from the MH+ ion of the peptides Tyr(Ala)9, (Ala)4Tyr(Ala)5, and (Ala)8TyrAla are essentially identical, indicative of full cyclization reaction to a common intermediate before fragmentation. This leads to abundant nondirect sequence ions in the product ion mass spectra of the b9 ions. The product ion mass spectra of the b8 ions from the first two peptides also are essentially identical. The fragmentation of the MH+ ions also leads to low intensity nondirect sequence ions in the product ion mass spectra. N-terminal acetylation blocks the cyclization and eliminates nondirect sequence fragment ions in the product ion mass spectra.



中文翻译:

肽 b9 离子的环化

通过从肽Tyr(Ala) 9、(Ala) 4 Tyr(Ala) 5和(Ala) 8 TyrAla的MH +离子损失中性丙氨酸而衍生的b 9离子的CID 获得的产物离子质谱是基本相同,表明在断裂前完全环化反应为共同的中间体。这导致 b 9离子的产物离子质谱中出现大量非直接序列离子。前两个肽段的 b 8离子的产物离子质谱图也基本相同。MH +的碎片化离子还会导致产物离子质谱图中的低强度非直接序列离子。N-末端乙酰化阻止环化并消除产物离子质谱中的非直接序列碎片离子。

更新日期:2020-03-01
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