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Mass spectrometry and computational study of ubiquitin associated with different metal (II) ions: Zinc, copper, nickel, cobalt, iron and manganese.

机译：遍在蛋白与不同金属（II）离子（锌，铜，镍，钴，铁和锰）相关的质谱分析和计算研究。

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Mass spectrometry (MS) is an analytical technique that measures the mass-to-charge ratio of charged particles. Mass spectrometry is an emerging tool used in the study of conformation, structure of protein and protein interactions with metal ions. Electrospray-Ionization (ESI) Mass Spectrometry is a "soft" ionization technique which can be used in the analysis of large biomolecules like proteins because of its ability to form singly to multiply charged ions. ESI can also be used to study interactions of proteins with metal ions and non covalent interactions in the tertiary structure, because these interactions often change the shape or conformations of proteins. Mass spectrometry has wide spread use in biological analyses, particularly in the areas of proteins, and characterization of large macromolecules. Positive charged metallated-ubiquitin protein ions produced by electrospray ionization are mass selected by a quadrupole mass analyzer and then fragmented by collision-induced dissociation in the ion trap cell and m/z measurement of the fragments are done using a time of flight mass analyzer. The ion mobility allows the separation of ions based on cross sectional area and helps to study the conformation of ubiquitin and metallated-ubiquitin at various charge states from 6+ to 9+.;Ubiquitin is a small 76 residue protein with a molecular weight of 8564.47 Da, which plays a key role in regulation of proteins by transferring the target proteins to proteosomes through the ubiquitin proteolysis cycle. The ubiquitin protein can interact with various metal ions. The interaction of ubiquitin with metal ions, the potential binding sites of metal ions, fragmentation of metallated-ubiquitin and conformational study of ubiquitin and metalated ubiquitin can be investigated by ESI-MS.

机译：质谱（MS）是一种分析技术，可测量带电粒子的质荷比。质谱法是一种新兴工具，用于研究蛋白质的构象，结构以及蛋白质与金属离子的相互作用。电喷雾电离（ESI）质谱技术是一种“软”电离技术，可用于分析大型生物分子（如蛋白质），因为它能够单独形成倍增带电离子的能力。 ESI还可以用于研究蛋白质与金属离子的相互作用以及三级结构中的非共价相互作用，因为这些相互作用通常会改变蛋白质的形状或构象。质谱在生物学分析中，特别是在蛋白质领域，以及大分子的表征中具有广泛的用途。由电喷雾电离产生的带正电的金属化泛素蛋白离子由四极杆质量分析仪进行质量选择，然后在离子阱池中通过碰撞诱导的离解进行碎裂，并使用飞行时间质量分析仪对碎片进行m / z测量。离子迁移率允许根据截面积分离离子，并有助于研究从6+到9+的各种电荷状态下的泛素和金属化泛素的构象。泛素是一种小的76残基蛋白质，分子量为8564.47。 Da，通过遍在蛋白的蛋白水解周期将靶蛋白转移到蛋白体中，在蛋白的调控中起着关键作用。泛素蛋白可以与各种金属离子相互作用。可以通过ESI-MS研究泛素与金属离子的相互作用，金属离子的潜在结合位点，金属化泛素的断裂以及泛素和金属化泛素的构象研究。

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作者
Nalla, Kiran Kumar.;
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Texas A&M University - Commerce.;

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授予单位 Texas A&M University - Commerce.;
学科 Biochemistry.;Analytical chemistry.;Inorganic chemistry.
学位 M.S.
年度 2012
页码 82 p.
总页数 82
原文格式 PDF
正文语种 eng
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Mass spectrometry and computational study of ubiquitin associated with different metal (II) ions: Zinc, copper, nickel, cobalt, iron and manganese.

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