期刊
BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS
卷 1861, 期 11, 页码 3053-3059出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbagen.2017.02.009
关键词
Enzyme electrostatics; Non-canonical amino acids; Enzyme catalysis; Electric fields; Vibrational Stark spectroscopy
资金
- DFG via Cluster of Excellence Unifying concepts in Catalysis [EXC 314]
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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