The role of phosphorylated residues in peptide-peptide noncovalent complexes formation.
The role of phosphorylated residues in peptide-peptide noncovalent complexes formation.
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DOI：
10.1016/j.jasms.2008.06.023
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发表时间：
2008-10
影响因子：
3.2
通讯作者：
Woods AS
中科院分区：
文献类型：
--
作者：
Jackson SN;Moyer SC;Woods AS
电喷雾质谱（ESI-MS）已成为研究非共价复合物的首选工具。我们以前的工作已经强调了磷酸化的氨基酸残基通过与精氨酸残基的胍基的静电相互作用在形成非共价复合物中的作用。在这项研究中，我们采用串联质谱研究这些非共价复合物的气相稳定性和解离途径。测试的三种磷酸肽的唯一差异是磷酸化氨基酸残基的性质。此外，酸性残基和酰胺化羧基末端的不存在确保了唯一的负电荷来自磷酸，这允许比较精氨酸残基和每个不同磷酸化残基之间的非共价键。通过绘制非共价络合离子强度作为进入碰撞池之前给予非共价络合离子的标称能量的函数来生成解离曲线。这些结果表明，与磷酸化酪氨酸形成的非共价复合物是最稳定的，其次是丝氨酸和苏氨酸，它们具有相似的稳定性。
Electrospray mass spectrometry (ESI-MS) has become the tool of choice for the study of noncovalent complexes. Our previous work has highlighted the role of phosphorylated amino acid residues in the formation of noncovalent complexes through electrostatic interaction with arginine residues’ guanidinium groups. In this study, we employ tandem mass spectrometry to investigate the gas-phase stability and dissociation pathways of these noncovalent complexes. The only difference in the three phosphopeptides tested is the nature of the phosphorylated amino acid residue. In addition the absence of acidic residues and an amidated carboxyl terminus insured that the only negative charge came from the phosphate, which allowed for the comparison of the nonconvalent bond between arginine residues and each of the different phosphorylated residues. Dissociation curves were generated by plotting noncovalent complex ion intensities as a function of the nominal energy given to the noncovalent complex ion prior to entering the collision cell. These results showed that noncovalent complexes formed with phosphorylated tyrosine were the most stable followed by serine and threonine which had similar stability.
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影响因子：
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通讯作者：
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