文章基本信息

标题：Pendular proteins in gases and new avenues for characterization of macromolecules by ion mobility spectrometry
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作者：Alexandre A. Shvartsburg ; Sergei Y. Noskov ; Randy W. Purves 等
期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：2009
卷号：106
期号：16
页码：6495-6500
DOI：10.1073/pnas.0812318106
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Polar molecules align in electric fields when the dipole energy (proportional to field intensity E x dipole moment p) exceeds the thermal rotational energy. Small molecules have low p and align only at inordinately high E or upon extreme cooling. Many biomacromolecules and ions are strong permanent dipoles that align at E achievable in gases and room temperature. The collision cross-sections of aligned ions with gas molecules generally differ from orientationally averaged quantities, affecting ion mobilities measured in ion mobility spectrometry (IMS). Field asymmetric waveform IMS (FAIMS) separates ions by the difference between mobilities at high and low E and hence can resolve and identify macroion conformers based on the mobility difference between pendular and free rotor states. The exceptional sensitivity of that difference to ion geometry and charge distribution holds the potential for a powerful method for separation and characterization of macromolecular species. Theory predicts that the pendular alignment of ions in gases at any E requires a minimum p that depends on the ion mobility, gas pressure, and temperature. At ambient conditions used in current FAIMS systems, p for realistic ions must exceed {approx}300-400 Debye. The dipole moments of proteins statistically increase with increasing mass, and such values are typical above {approx}30 kDa. As expected for the dipole-aligned regime, FAIMS analyses of protein ions and complexes of {approx}30-130 kDa show an order-of-magnitude expansion of separation space compared with smaller proteins and other ions.
关键词：mass spectrometry ; protein structure