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An expanded genetic code for probing the role of electrostatics in enzyme catalysis by vibrational Stark spectroscopy
Citation key ISI:000415778700014
Author Voeller, Jan-Stefan and Biava, Hernan and Hildebrandt, Peter and Budisa, Nediljko
Pages 3053-3059
Year 2017
ISSN 0304-4165
DOI 10.1016/j.bbagen.2017.02.009
Volume 1861
Number 11, B, SI
Month NOV
Abstract Background: 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. Scope of review: 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. Major conclusions: 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. General significance: 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. Illca Heinemann and Dr. Patrick O'Donoghue. (c) 2017 Elsevier B.V. All rights reserved.
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