MASS-SPECTROMETRIC STUDIES ON NONCOVALENT DIMERS OF LEUCINE-ZIPPER PEPTIDES
MASS-SPECTROMETRIC STUDIES ON NONCOVALENT DIMERS OF LEUCINE-ZIPPER PEPTIDES
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DOI：
10.1021/ja00071a058
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发表时间：
1993-09-08
影响因子：
15
通讯作者：
GANEM, B
中科院分区：
文献类型：
--
作者：
LI, YT;HSIEH, YL;GANEM, B
亮氨酸拉链存在于几种DNA结合蛋白中，它代表了一个非共价二聚基序，以增强DNA结合。采用在线体积排阻液相色谱-离子喷雾质谱法证实了亮氨酸拉链多肽Gcn4-p1和N16V的溶液二聚反应。串联质谱学研究表明，气相中也存在二聚体离子。高分辨率的俘获离子研究表明，这些气态二聚体至少可以稳定几分钟。与它们在水溶液中的行为定性一致，N16V比GCN4-p1更倾向于形成二聚体，后者出人意料地与杂质形成非共价异二聚体。
The leucine zipper, found in several DNA-binding proteins, represents a motif for noncovalent dimerization to enhance DNA binding. Solution dimerization of the leucine zipper peptides GCN4-p1 and N16V is confirmed here by on-line, size-exclusion liquid chromatography-ion spray mass spectrometry. Tandem mass spectrometry studies indicate that dimer ions also exist in the gas phase. High-resolution trapped-ion studies show that these gaseous dimers are stable for at least minutes. In qualitative agreement with their behavior in aqueous solution, N16V has a greater tendency to form dimers than does GCN4-p1, which unexpectedly forms a noncovalent heterodimer with an impurity.