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An expanded genetic code for probing the role of electrostatics in enzyme catalysis by vibrational Stark spectroscopy
Zitatschlüssel 159.2017.Völler
Autor Völler J.-S., and Biava, H., and Hildebrandt, P., and Budisa, N.
Jahr 2017
DOI doi: 10.1016/j.bbagen.2017.02.009.doi.org
Journal Biochim. Biophys. Acta
Jahrgang [Epub ahead of print]
Zusammenfassung 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. Ilka Heinemann and Dr. Patrick O'Donoghue. Copyright © 2017 Elsevier B.V. All rights reserved.
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