紫外光解吸质谱法增强膜蛋白复合物的特性描述。
Enhanced Characterization of Membrane Protein Complexes by Ultraviolet Photodissociation Mass Spectrometry.
机构信息
Department of Chemistry , University of Texas at Austin , Austin , Texas 78712 , United States.
Department of Chemistry , Texas A&M University , College Station , Texas 77842 , United States.
出版信息
Anal Chem. 2020 Jan 7;92(1):899-907. doi: 10.1021/acs.analchem.9b03689. Epub 2019 Dec 10.
Abstract
Development of chemical chaperones to solubilize membrane protein complexes in aqueous solutions has allowed for gas-phase analysis of their native-like assemblies, including rapid evaluation of stability and interacting partners. Characterization of protein primary sequence, however, has thus far been limited. Ultraviolet photodissociation (UVPD) generates a multitude of sequence ions for the ammonia channel (AmtB), provides improved localization of a possible post-translational modification of aquaporin Z (AqpZ), and surpasses previous reports of sequence coverage for mechanosensitive channel of large conductance (MscL). Variations in UVPD sequence ion abundance have been shown to correspond to structural changes induced upon some perturbation. Preliminary results are reported here for elucidating increased rigidity or flexibility of MscL when bound to various phospholipids.
摘要
化学伴侣的发展使得膜蛋白复合物能够在水溶液中溶解，从而可以对其类似天然状态的组装体进行气相分析，包括快速评估其稳定性和相互作用伙伴。然而，到目前为止，对蛋白质一级序列的表征还很有限。 紫外线光解（UVPD）为氨通道（AmtB）产生了大量的序列离子，提供了对水通道蛋白 Z（AqpZ）的可能翻译后修饰的更好定位，并且超过了先前报道的大电导机械敏感通道（MscL）的序列覆盖率。已经表明，紫外线光解序列离子丰度的变化与某些扰动诱导的结构变化相对应。这里报告了初步结果，阐明了当与各种磷脂结合时，MscL 的刚性或柔性增加。
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