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通过2H魔角旋转固态核磁共振光谱法研究含甲基氘代α-氨基异丁酸的肽菌素的膜结合构象。

Membrane-bound conformation of peptaibols with methyl-deuterated alpha-amino isobutyric acids by 2H magic angle spinning solid-state NMR spectroscopy.

作者信息

Bertelsen Kresten, Pedersen Jan M, Rasmussen Brian S, Skrydstrup Troels, Nielsen Niels Chr, Vosegaard Thomas

机构信息

Center for Insoluble Protein Structures (inSPIN), Interdisciplinary Nanoscience Center (iNANO) and Department of Chemistry, University of Aarhus, Langelandsgade 140, DK-8000 Aarhus C, Denmark.

出版信息

J Am Chem Soc. 2007 Nov 28;129(47):14717-23. doi: 10.1021/ja0749690. Epub 2007 Nov 7.

Abstract

We present the use of 2H magic-angle spinning (MAS) NMR on methyl-deuterated alpha-amino isobutyric acid (Aib) as a new method to obtain fast and accurate structural constraints on peptaibols in membrane-bound environments. Using nonoriented vesicle-reconstituted samples we avoid the delicate preparation of oriented samples, and the use of MAS ensures high sensitivity and thereby very fast acquisition of experimental spectra. Furthermore, given the high content ( approximately 40%) of Aib in peptaibols and the fact that the amino acid Aib may be synthesized from cheap starting materials, even in the case of 2H, 13C, or 15N labeling, this method is ideally suited for studies of the membrane-bound conformation of peptaibols.

摘要

我们展示了使用2H魔角旋转(MAS)核磁共振技术对甲基氘代α-氨基异丁酸(Aib)进行研究,以此作为一种在膜结合环境中获取肽抗生素快速准确结构限制的新方法。使用非定向囊泡重构样品,我们避免了定向样品的精细制备,并且MAS的使用确保了高灵敏度,从而能够非常快速地采集实验光谱。此外,鉴于肽抗生素中Aib的含量很高(约40%),以及氨基酸Aib可以由廉价起始原料合成这一事实,即使在2H、13C或15N标记的情况下,该方法也非常适合用于研究肽抗生素的膜结合构象。

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