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Solid-state protein-structure determination with proton-detected triple-resonance 3D magic-angle-spinning NMR spectroscopy.利用质子检测的三重共振三维魔角旋转核磁共振光谱法进行固态蛋白质结构测定。
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2
Proton-detected solid-state NMR spectroscopy of fully protonated proteins at 40 kHz magic-angle spinning.在40千赫兹魔角旋转条件下对完全质子化蛋白质进行质子检测的固态核磁共振光谱学。
J Am Chem Soc. 2007 Sep 26;129(38):11791-801. doi: 10.1021/ja073462m. Epub 2007 Aug 29.
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Observation of heteronuclear overhauser effects confirms the 15N-1H dipolar relaxation mechanism in a crystalline protein.异核Overhauser效应的观察证实了晶体蛋白中的15N-1H偶极弛豫机制。
J Am Chem Soc. 2006 Sep 27;128(38):12398-9. doi: 10.1021/ja064037g.
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Investigation of dipolar-mediated water-protein interactions in microcrystalline Crh by solid-state NMR spectroscopy.通过固态核磁共振光谱法研究微晶Crh中偶极介导的水-蛋白质相互作用。
J Am Chem Soc. 2006 Jun 28;128(25):8246-55. doi: 10.1021/ja060866q.
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Ultrahigh resolution in proton solid-state NMR spectroscopy at high levels of deuteration.高氘代水平下质子固态核磁共振光谱中的超高分辨率。
Angew Chem Int Ed Engl. 2006 Jun 2;45(23):3878-81. doi: 10.1002/anie.200600328.
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Magic-angle spinning solid-state NMR spectroscopy of the beta1 immunoglobulin binding domain of protein G (GB1): 15N and 13C chemical shift assignments and conformational analysis.蛋白质G(GB1)的β1免疫球蛋白结合结构域的魔角旋转固态核磁共振光谱:15N和13C化学位移归属及构象分析
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Protein structure determination by high-resolution solid-state NMR spectroscopy: application to microcrystalline ubiquitin.通过高分辨率固态核磁共振光谱法测定蛋白质结构:应用于微晶泛素。
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Detection of dynamic water molecules in a microcrystalline sample of the SH3 domain of alpha-spectrin by MAS solid-state NMR.通过魔角旋转固态核磁共振技术检测α-血影蛋白SH3结构域微晶样品中的动态水分子。
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用于质子检测固态核磁共振的高性能溶剂抑制

High-performance solvent suppression for proton detected solid-state NMR.

作者信息

Zhou Donghua H, Rienstra Chad M

机构信息

Department of Chemistry, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA.

出版信息

J Magn Reson. 2008 May;192(1):167-72. doi: 10.1016/j.jmr.2008.01.012. Epub 2008 Feb 1.

DOI:10.1016/j.jmr.2008.01.012
PMID:18276175
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2443633/
Abstract

High-sensitivity proton detected experiments in solid-state NMR have been recently demonstrated in proton diluted proteins as well as fully protonated samples under fast magic-angle spinning. One key element for performing successful proton detection is effective solvent suppression achieved by pulsed field gradients (PFG) and/or saturation pulses. Here we report a high-performance solvent suppression method that attenuates multiple solvent signals simultaneously by more than a factor of 10,000, achieved by an optimized combination of homospoil gradients and supercycled saturation pulses. This method, which we call Multiple Intense Solvent Suppression Intended for Sensitive Spectroscopic Investigation of Protonated Proteins, Instantly (MISSISSIPPI), can be applied without a PFG probe. It opens up new opportunities for two-dimensional heteronuclear correlation spectroscopy of hydrated proteins at natural abundance as well as high-sensitivity and multi-dimensional experimental investigation of protein-solvent interactions.

摘要

最近,在快速魔角旋转条件下,高灵敏度质子检测实验已在质子稀释蛋白以及完全质子化样品的固态核磁共振中得到证实。成功进行质子检测的一个关键要素是通过脉冲场梯度(PFG)和/或饱和脉冲实现有效的溶剂抑制。在此,我们报告一种高性能溶剂抑制方法,该方法通过同相破坏梯度和超循环饱和脉冲的优化组合,能同时将多个溶剂信号衰减至10000倍以上。我们将此方法称为用于质子化蛋白质敏感光谱研究的即时多重强溶剂抑制(MISSISSIPPI),它无需PFG探头即可应用。这为天然丰度下的水合蛋白二维异核相关光谱以及蛋白质 - 溶剂相互作用的高灵敏度和多维实验研究开辟了新机遇。