期刊
ANALYTICAL CHEMISTRY
卷 85, 期 14, 页码 6967-6973出版社
AMER CHEMICAL SOC
DOI: 10.1021/ac4015963
关键词
-
资金
- NIH NIGMS [8 P41 GM103493-10]
- US DOE OBER
Proteins in solution or the gas phase tend to exhibit multiple conformational families, each comprising distinct structures. Separation methods have generally failed to resolve these, with their convolution producing wide peaks. Here, we report full separation of > 10 conformers for most ubiquitin charge states by the new approach of differential ion mobility spectrometry (field asymmetric waveform ion mobility spectrometry, FAIMS) employing H-2/N-2 gas mixtures with up to 85% H-2. The resolving power (up to 400) is five times the highest previously achieved (using He/N-2 buffers), greatly increasing the separation specificity. The peak widths match the narrowest obtained by FAIMS for any species under the same conditions and scale with the protein charge state (z) and ion residence time (t) as z(-1/2) and t(-1/2), as prescribed for instrumental (diffusional) broadening. This suggests resolution of specific geometries rather than broader ensembles.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据