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Cover Feature: Impact of Azidohomoalanine Incorporation on Protein Structure and Ligand Binding (ChemBioChem 23/2017)
ChemBioChem ( IF 3.2 ) Pub Date : 2017-11-21 , DOI: 10.1002/cbic.201700603
Florian Lehner 1 , Denis Kudlinzki 1, 2 , Christian Richter 1 , Henrike M. Müller-Werkmeister 3 , Katharina B. Eberl 3 , Jens Bredenbeck 3 , Harald Schwalbe 1 , Robert Silvers 1, 4
Affiliation  

The cover feature picture shows the structure of the unnatural amino acid–modified PDZ3 domain, which was thoroughly investigated by NMR spectroscopy and X‐ray crystallography. Azidohomoalanine was introduced by expression in methionine auxotrophic cells to study the impact of the incorporation of an unnatural amino acid on protein structure, dynamics, and ligand binding properties. The results led to the formulation of a flexible guideline that could help researchers that study systems containing unnatural amino acids. More information can be found in the full paper by H. Schwalbe, R. Silvers, et al. on page 2340 in Issue 23, 2017 (DOI: 10.1002/cbic.201700437).
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中文翻译:

封面人物:叠氮高苏氨酸的掺入对蛋白质结构和配体结合的影响(ChemBioChem 23/2017)

封面特征图片显示了非天然氨基酸修饰的PDZ3结构域的结构,已通过NMR光谱学和X射线晶体学对其进行了彻底研究。通过在蛋氨酸营养缺陷型细胞中的表达引入叠氮高丙氨酸,以研究掺入非天然氨基酸对蛋白质结构,动力学和配体结合特性的影响。结果导致制定了灵活的指南,可以帮助研究人员研究含有非天然氨基酸的系统。更多信息可以在H. Schwalbe,R。Silvers等人的全文中找到。就在第23期,2017年2340页(:10.1002 / cbic.201700437 DOI)。
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更新日期:2017-11-21
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