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L-赖氨酸:利用粉末 X 射线衍射完成 20 种直接编码蛋白质氨基酸的晶体结构集合。

L-Lysine: exploiting powder X-ray diffraction to complete the set of crystal structures of the 20 directly encoded proteinogenic amino acids.

机构信息

School of Chemistry, Cardiff University, Cardiff CF10 3AT, Wales (UK).

出版信息

Angew Chem Int Ed Engl. 2015 Mar 23;54(13):3973-7. doi: 10.1002/anie.201411520. Epub 2015 Feb 4.

Abstract

During the last 75 years, crystal structures have been reported for 19 of the 20 directly encoded proteinogenic amino acids in their natural (enantiomerically pure) form. The crystal structure is now reported for the final member of this set: L-lysine. As crystalline L-lysine has a strong propensity to incorporate water under ambient atmospheric conditions to form a hydrate phase, the pure (non-hydrate) crystalline phase can be obtained only by dehydration under rigorously anhydrous conditions, resulting in a microcrystalline powder sample. For this reason, modern powder X-ray diffraction methods have been exploited to determine the crystal structure in this final, elusive case.

摘要

在过去的 75 年中,已有 19 种天然(对映体纯)形式的直接编码蛋白氨基酸的晶体结构被报道。本文报告了该系列的最后一个成员:L-赖氨酸。由于结晶 L-赖氨酸在环境大气条件下强烈倾向于结合水形成水合相,因此只有在严格无水条件下进行脱水才能获得纯(非水合)结晶相,从而得到微晶粉末样品。出于这个原因,现代粉末 X 射线衍射方法已被用于确定这最后一个难以捉摸的案例的晶体结构。

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