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本文引用的文献

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Solid-state NMR triple-resonance backbone assignments in a protein.蛋白质中固态核磁共振三共振主链归属
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Structures of the M2 channel-lining segments from nicotinic acetylcholine and NMDA receptors by NMR spectroscopy.通过核磁共振光谱法测定烟碱型乙酰胆碱受体和NMDA受体的M2通道内衬片段的结构。
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NMR structural studies of membrane proteins.膜蛋白的核磁共振结构研究。
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From muscle endplate to brain synapses: a short history of synapses and agonist-activated ion channels.从肌肉终板到脑突触：突触与激动剂激活离子通道简史
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Solid-state NMR studies of the membrane-bound closed state of the colicin E1 channel domain in lipid bilayers.脂质双分子层中大肠杆菌素E1通道结构域膜结合封闭状态的固态核磁共振研究。
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Pathological mutations of nicotinic receptors and nicotine-based therapies for brain disorders.烟碱型受体的病理突变与基于尼古丁的脑部疾病治疗方法
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Complete resolution of the solid-state NMR spectrum of a uniformly 15N-labeled membrane protein in phospholipid bilayers.磷脂双分子层中均匀15N标记的膜蛋白固态核磁共振谱的完全解析。
Proc Natl Acad Sci U S A. 1997 Aug 5;94(16):8551-6. doi: 10.1073/pnas.94.16.8551.
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Magic angle spinning NMR spectroscopy of membrane proteins.膜蛋白的魔角旋转核磁共振光谱学。
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High-resolution NMR of biological solids.生物固体的高分辨率核磁共振
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Three-dimensional solid-state NMR correlation experiment with 1H homonuclear spin exchange.具有1H同核自旋交换的三维固态核磁共振相关实验
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定向蛋白质固态核磁共振谱的稀释自旋交换归属：双层膜中的乙酰胆碱M2

Dilute spin-exchange assignment of solid-state NMR spectra of oriented proteins: acetylcholine M2 in bilayers.

作者信息

Marassi F M, Gesell J J, Valente A P, Kim Y, Oblatt-Montal M, Montal M, Opella S J

机构信息

Department of Chemistry, University of Pennsylvania, Philadelphia 19104, USA.

出版信息

J Biomol NMR. 1999 Jun;14(2):141-8. doi: 10.1023/a:1008391823293.

DOI:10.1023/a:1008391823293
PMID:10427741
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3282054/
Abstract

The assignment of amide resonances in the two-dimensional PISEMA (Polarization Inversion with Spin Exchange at the Magic Angle) spectrum of uniformly 15N labeled M2 peptide corresponding to the channel-lining segment of the acetylcholine receptor in oriented phospholipid bilayers is described. The majority of the resonances were assigned through comparisons with spectra from selectively 15N labeled recombinant peptides and specifically 15N labeled synthetic peptides. Some resonances were assigned to specific amino acid residues by means of homonuclear 15N spin-exchange spectroscopy. A modification to the conventional spin-exchange pulse sequence that significantly shortens the length of the experiments by combining the intervals for 15N spin-exchange and 1H magnetization recovery is described.

摘要

描述了在取向磷脂双层中对应于乙酰胆碱受体通道内衬段的均匀15N标记的M2肽的二维PISEMA（魔角自旋交换极化反转）谱中酰胺共振的归属。通过与选择性15N标记的重组肽和特异性15N标记的合成肽的光谱进行比较，确定了大多数共振峰。通过同核15N自旋交换光谱法将一些共振峰归属到特定的氨基酸残基。描述了对传统自旋交换脉冲序列的一种改进，该改进通过结合15N自旋交换和1H磁化恢复的时间间隔，显著缩短了实验时长。