タンパク質の構造と機能を質量分析で解明する : —イオンモビリティー質量分析によるプリオンタンパク質の解析—

概要

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Applications of traveling-wave ion mobility (T-Wave-IM) and drift cell ion mobility (DCIM) mass spectrometry to studies of prion proteins are summarized. In ion mobility spectrometry, ions that are produced travel through a drift tube to which has an electric field is applied and a carrier buffer gas that opposes the motion of the ions. Based on the mass, charge, size and shape, and the migration time of an ion through the tube is unique to each different ion. This permits the operator to distinguish between different analyte species. Compact ions with small collision cross-sections will drift more rapidly than extended ions. The measurement of this mobility yields information regarding the rotationally-averaged cross-section of each ion. Separation of α-helical and β-sheet-rich SHaPrP(90-231) isoforms of recombinant Syrian hamster prion proteins, with the same m/z but different structures, can be achieved via the use of ion mobility data.