Dynamic Nuclear Polarization of Biomembrane Assemblies.

Dynamic Nuclear Polarization of Biomembrane Assemblies.
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生物膜组件的动态核极化。

DOI:
10.3390/biom10091246
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发表时间:
2020-08-27
期刊:
影响因子:
5.5
通讯作者:
Long JR
Long JR
中科院分区:
生物学2区
文献类型:
--
作者:
Tran NT;Mentink-Vigier F;Long JR

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虽然原子尺度的结构和动态信息是核磁共振(NMR)方法的标志,但灵敏度是核磁共振研究的一个基本限制。充分利用核磁共振的能力来研究膜蛋白进一步阻碍了它们在生物膜内的稀释。动态核极化(DNP)可以将相对高极化的未配对电子转移到核自旋上,这一技术的最新进展有望克服灵敏度瓶颈,并使膜蛋白在天然条件下的核磁共振表征成为可能。在这里,我们讨论了dnp增强固态核磁共振波谱的基本方面,与脂质组装和结合蛋白研究相关的实验细节,以及可以在生物膜样品中实现的灵敏度增益。我们还提出了从DNP测量中可以获得的独特见解,并展望了在天然脂质环境中阐明膜蛋白结构和取向的技术的进一步发展。
While atomic scale structural and dynamic information are hallmarks of nuclear magnetic resonance (NMR) methodologies, sensitivity is a fundamental limitation in NMR studies. Fully exploiting NMR capabilities to study membrane proteins is further hampered by their dilution within biological membranes. Recent developments in dynamic nuclear polarization (DNP), which can transfer the relatively high polarization of unpaired electrons to nuclear spins, show promise for overcoming the sensitivity bottleneck and enabling NMR characterization of membrane proteins under native-like conditions. Here we discuss fundamental aspects of DNP-enhanced solid-state NMR spectroscopy, experimental details relevant to the study of lipid assemblies and incorporated proteins, and sensitivity gains which can be realized in biomembrane-based samples. We also present unique insights which can be gained from DNP measurements and prospects for further development of the technique for elucidating structures and orientations of membrane proteins in native lipid environments.
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