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Impact of Azidohomoalanine Incorporation on Protein Structure and Ligand Binding
ChemBioChem ( IF 2.6 ) Pub Date : 2017-11-07 06:06:33 , DOI: 10.1002/cbic.201700437
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  

Unnatural influence: Unnatural amino acids are widely used to study proteins. NMR spectroscopy and X-ray diffraction are applied to characterize the structural and dynamic impact of azidohomoalanine (AZH) incorporation into the model protein PDZ3 domain. The structure and dynamics of the apo state of AZH-modified PDZ3 remains mostly unperturbed.

中文翻译:

叠氮高丙氨酸掺入对蛋白质结构和配体结合的影响

非自然的影响:非自然的氨基酸被广泛用于研究蛋白质。NMR光谱和X射线衍射用于表征将叠氮高丙氨酸(AZH)掺入模型蛋白质PDZ3结构域的结构和动态影响。AZH修饰的PDZ3的apo态的结构和动力学仍然保持稳定。
更新日期:2017-11-07
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