Department of Chemistry, Technische Universität Berlin, Müller-Breslau-Strasse 10, D-10623 Berlin, Germany.
Department of Chemistry, Technische Universität Berlin, Müller-Breslau-Strasse 10, D-10623 Berlin, Germany; Department of Chemistry, Technische Universität Berlin, Straße des 17. Juni 135, D-10623 Berlin, Germany.
Biochim Biophys Acta Gen Subj. 2017 Nov;1861(11 Pt B):3053-3059. doi: 10.1016/j.bbagen.2017.02.009. Epub 2017 Feb 14.
To find experimental validation for electrostatic interactions essential for catalytic reactions represents a challenge due to practical limitations in assessing electric fields within protein structures.
This review examines the applications of non-canonical amino acids (ncAAs) as genetically encoded probes for studying the role of electrostatic interactions in enzyme catalysis.
ncAAs constitute sensitive spectroscopic probes to detect local electric fields by exploiting the vibrational Stark effect (VSE) and thus have the potential to map the protein electrostatics.
Mapping the electrostatics in proteins will improve our understanding of natural catalytic processes and, in beyond, will be helpful for biocatalyst engineering. This article is part of a Special Issue entitled "Biochemistry of Synthetic Biology - Recent Developments" Guest Editor: Dr. Ilka Heinemann and Dr. Patrick O'Donoghue.
由于在评估蛋白质结构内电场方面存在实际限制，因此寻找对催化反应至关重要的静电相互作用的实验验证是一项挑战。
本文综述了非天然氨基酸（ncAAs）作为遗传编码探针在研究静电相互作用在酶催化中的作用中的应用。
ncAAs 通过利用振动斯塔克效应（VSE）构成了灵敏的光谱探针，以检测局部电场，因此有可能绘制蛋白质静电图。
绘制蛋白质中的静电图将有助于我们理解自然催化过程，并且在超越自然的范围内，对于生物催化剂工程也将有所帮助。本文是题为“合成生物学的生物化学-最新进展”的特刊的一部分，客座编辑：Ilka Heinemann 博士和 Patrick O'Donoghue 博士。
