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通过离子淌度和自由基探针 MS 研究 βB2B3-晶体蛋白异二聚体的同源建模结构。

Homology-modelled structure of the βB2B3-crystallin heterodimer studied by ion mobility and radical probe MS.

机构信息

School of Molecular Bioscience, University of Sydney, Sydney, Australia.

出版信息

FEBS J. 2011 Nov;278(21):4044-54. doi: 10.1111/j.1742-4658.2011.08309.x. Epub 2011 Sep 15.

DOI:10.1111/j.1742-4658.2011.08309.x
PMID:21848669
Abstract

Ion mobility MS was employed to study the structure of the βB2B3-crystallin heterodimer following its detection by ESI-TOF MS. The results demonstrate that the heterodimer has a similar cross-section (3 165 Å(2)) and structure to the βB2B2-crystallin homodimer. Several homology-modelled structures for the βB2B3 heterodimer were constructed and assessed in terms of their calculated collision cross-sections and whether the solvent accessibilities of reactive amino acid side chains throughout the βB3 subunit are in accord with measured oxidation levels in radical probe MS protein footprinting experiments. The βB2B3 heterodimer AD model provides the best representation of the heterodimer's structure overall following a consideration of both the ion mobility and radical probe MS data.

摘要

离子淌度 MS 被用于研究 ESI-TOF MS 检测到的 βB2B3-晶体蛋白异二聚体的结构。结果表明,异二聚体具有相似的截面(3165Å2)和结构βB2B2-晶体蛋白同二聚体。构建了几种βB2B3 异二聚体的同源建模结构,并根据其计算的碰撞截面以及βB3 亚基中反应性氨基酸侧链的溶剂可及性是否与自由基探针 MS 蛋白质足迹实验中测量的氧化水平一致进行了评估。βB2B3 异二聚体 AD 模型在综合考虑离子淌度和自由基探针 MS 数据后,提供了对异二聚体结构的最佳整体表示。

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