New method to study the effects of peptide sequence on the dissociation energetics of peptide ions.

New method to study the effects of peptide sequence on the dissociation energetics of peptide ions.
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研究肽序列对肽离子解离能量影响的新方法。

DOI:
10.1016/s1044-0305(97)00281-x
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发表时间:
1998
影响因子:
3.2
通讯作者:
Glish,GL
Glish,GL
中科院分区:
化学3区
文献类型:
--
作者:
Vachet,RW;Glish,GL

文献摘要

相似文献

发展了一种用四极离子陷阱质谱仪研究单质子化多肽解离模式的新方法。新的方法包括使用边界激活的解离来表征多肽离子的解离的容易程度。可以深入了解特定的多肽序列对质子化多肽的解离能的影响。对特定序列对多肽离子解离模式的影响的了解的增加,应该会提高从串联质谱学(MS/MS)实验中解释复杂光谱的能力。这种方法证实了先前观察到的含有碱性残基的多肽离子解离所需的能量增加。此外,该技术还揭示了脯氨酸残基的位置对多肽与该氨基酸的解离能的影响。
A new method has been developed to study the dissociation patterns of singly protonated peptides by using a quadrupole ion trap mass spectrometer. The new approach involves using boundary-activated dissociation to characterize the ease of dissociation of peptide ions. Insight can be gained into the effect of specific peptide sequences on the dissociation energetics of protonated peptides. Increased knowledge of the effects of specific sequences on the dissociation patterns of peptide ions should improve the ability to interpret complex spectra from tandem mass spectrometry (MS/MS) experiments. This method has confirmed the previously observed increase in the energy needed for the dissociation of peptide ions containing basic residues. In addition, this technique has revealed the effect of the location of proline residues on the dissociation energetics of peptides with this amino acid.