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Published April 7, 2016 | Supplemental Material
Journal Article Open

Photoelectrochemical Behavior of n-Type GaAs(100) Electrodes Coated by a Single Layer of Graphene

Abstract

Methods for cell-selective analysis of proteome dynamics will facilitate studies of biological processes in multicellular organisms. Here we describe a mutant murine methionyl-tRNA synthetase (designated L274GMmMetRS) that charges the noncanonical amino acid azidonorleucine (Anl) to elongator tRNA^(Met) in hamster (CHO), monkey (COS7), and human (HeLa) cell lines. Proteins made in cells that express the synthetase can be labeled with Anl, tagged with dyes or affinity reagents, and enriched on affinity resin to facilitate identification by mass spectrometry. The method does not require expression of orthogonal tRNAs or depletion of canonical amino acids. Successful labeling of proteins with Anl in several mammalian cell lines demonstrates the utility of L274GMmMetRS as a tool for cell-selective analysis of mammalian protein synthesis.

Additional Information

© 2016 American Chemical Society. Received: January 8, 2016. Revised: March 8, 2016. Publication Date (Web): March 10, 2016. N.S.L. and F.Y. acknowledge support from the U.S. Department of Energy Office of Basic Energy Sciences, Grant DE-FG02-03ER15483, the Defense Advanced Research Projects Agency (DARPA) Grant W911NF-09-2-0011, and the Gordon and Betty Moore Foundation, grant 1225, for support, and the Beckman Institute Molecular Materials Resource Center for facilities. A.C.N. acknowledges support from NSF graduate research fellowship. The authors thank Dr. Nicholas Petrone and Professor James Hone of Columbia University for providing the graphene samples and K. Papadantonakis for assistance with editing this manuscript. The authors declare no competing financial interest.

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