CONFORMATIONAL IMPLICATIONS OF ASPARAGINE-LINKED GLYCOSYLATION
CONFORMATIONAL IMPLICATIONS OF ASPARAGINE-LINKED GLYCOSYLATION
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DOI：
10.1073/pnas.92.1.97
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发表时间：
1995-01-03
影响因子：
11.1
通讯作者：
RICKERT, KW
中科院分区：
文献类型：
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作者：
IMPERIALI, B;RICKERT, KW
共翻译蛋白质修饰对蛋白质折叠过程的影响知之甚少。时间分辨荧光能量转移已用于评估糖基化对柔性寡肽构象动力学的影响。所检查的肽序列选自已知三维结构的糖蛋白。与 N 连接糖基化相关的能量传递调节与在水中采样不同构象的糖肽一致。结果表明，糖基化导致修饰的肽采用不同的构象集合，并且对于某些肽，这种变化可能导致构象更紧凑并且更接近最终折叠蛋白质中这些肽的构象。这一结果进一步表明，共翻译糖基化可以触发结构成核元件的及时形成，从而有助于蛋白质折叠的复杂过程。
The effects of cotranslational protein modification on the process of protein folding are poorly understood. Time-resolved fluorescence energy transfer has been used to assess the impact of glycosylation on the conformational dynamics of flexible oligopeptides. The peptide sequences examined are selected from glycoproteins of known three-dimensional structure. The energy transfer modulation associated with N-linked glycosylation is consistent with the glycopeptides sampling different conformational profiles in water. Results show that glycosylation causes the modified peptides to adopt a different ensemble of conformations, and for some peptides this change may lead to conformations that are more compact and better approximate the conformation of these peptides in the final folded protein. This result further implies that cotranslational glycosylation can trigger the timely formation of structural nucleation elements and thus assist in the complex process of protein folding.