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使用红外光谱和固态 NMR 光谱测量对取向样品进行研究，深入了解肽纳米管的分子结构。

Insights into the molecular architecture of a peptide nanotube using FTIR and solid-state NMR spectroscopic measurements on an aligned sample.

机构信息

Institute of Integrative Biology, University of Liverpool, Crown Street, Liverpool L69 7ZB (UK).

出版信息

Angew Chem Int Ed Engl. 2013 Sep 27;52(40):10537-40. doi: 10.1002/anie.201301960. Epub 2013 Aug 16.

DOI:10.1002/anie.201301960
PMID:23955926
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC4672711/
Abstract

Queuing up: Molecular orientation within macroscopically aligned nanotubes of the peptide AAAAAAK can be studied by solid-state NMR and IR spectroscopy. Line shape analysis of the NMR spectra indicates that the peptide N-H bonds are tilted 65-70° relative to the nanotube long axis. Re-evaluation of earlier X-ray fiber diffraction data suggests that the peptide molecules are hydrogen-bonded in a helical arrangement along the nanotube axis.

摘要

排队

通过固态 NMR 和红外光谱可以研究多肽 AAAAAAK 的宏观排列纳米管内的分子取向。NMR 谱线形状分析表明，肽的 N-H 键相对于纳米管长轴倾斜 65-70°。对早期 X 射线纤维衍射数据的重新评估表明，肽分子沿纳米管轴以氢键方式呈螺旋排列。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/75ab/4672711/9c57cd8cc664/anie0052-10537-f4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/75ab/4672711/0a944239706f/anie0052-10537-f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/75ab/4672711/e4132bbcb6d5/anie0052-10537-f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/75ab/4672711/276d2f9e3da1/anie0052-10537-f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/75ab/4672711/9c57cd8cc664/anie0052-10537-f4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/75ab/4672711/0a944239706f/anie0052-10537-f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/75ab/4672711/e4132bbcb6d5/anie0052-10537-f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/75ab/4672711/276d2f9e3da1/anie0052-10537-f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/75ab/4672711/9c57cd8cc664/anie0052-10537-f4.jpg

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