Methods of structural mass spectrometry have become more popular to study protein structure and dynamics. Among them, fast photochemical oxidation of proteins (FPOP) has several advantages such as irreversibility of modifications and more facile determination of the site of modification with single residue resolution. In the present study, FPOP analysis was applied to study the hemoglobin (Hb) – haptoglobin (Hp) complex allowing identification of respective regions altered upon the complex formation. Oxidative modifications were precisely localized on specific residues using a timsTOF Pro mass spectrometer. The data allowed determination of amino acids directly involved in Hb – Hp interactions and those located outside of the interaction interface yet affected by the complex formation. Data are available via ProteomeXchange with identifier PXD021621.

中文翻译：

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人类触珠蛋白-血红蛋白复合物的羟基自由基足迹分析

结构质谱方法在研究蛋白质结构和动力学方面变得越来越流行。其中，蛋白质的快速光化学氧化 (FPOP) 具有几个优点，例如修饰的不可逆性和更容易确定修饰位点的单残基分辨率。在本研究中，FPOP 分析用于研究血红蛋白 (Hb) - 触珠蛋白 (Hp) 复合物，从而可以识别复合物形成时发生变化的各个区域。使用 timsTOF Pro 质谱仪将氧化修饰精确定位在特定残基上。该数据允许确定直接参与 Hb-Hp 相互作用的氨基酸以及位于相互作用界面之外但受复合物形成影响的氨基酸。