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| 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 |
| Journal | BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS |
| 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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