Communication

Biosynthetic Incorporation of Fluorohistidine into Proteins in E. coli: A New Probe of Macromolecular Structure

  1. Jack F. Eichler Dr.1,
  2. John C. Cramer Dr.2,
  3. Kenneth L. Kirk Dr.2,
  4. James G. Bann Prof. Dr.1

Article first published online: 31 OCT 2005

DOI: 10.1002/cbic.200500249

Issue

ChemBioChem

ChemBioChem

Volume 6, Issue 12, pages 2170–2173, December 2, 2005

Additional Information

How to Cite

Eichler, J. F., Cramer, J. C., Kirk, K. L. and Bann, J. G. (2005), Biosynthetic Incorporation of Fluorohistidine into Proteins in E. coli: A New Probe of Macromolecular Structure. ChemBioChem, 6: 2170–2173. doi: 10.1002/cbic.200500249

Author Information

  1. 1

    Department of Chemistry, Wichita State University, Wichita, KS 67226, USA, Fax: (+1) 316-978-7373

  2. 2

    Laboratory of Bioorganic Chemistry, National Institute of Diabetes & Digestive & Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA

Publication History

  1. Issue published online: 30 NOV 2005
  2. Article first published online: 31 OCT 2005
  3. Manuscript Received: 10 JUN 2005

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Keywords:

  • amino acids;
  • biosynthesis;
  • fluorine;
  • histidine;
  • protein modifications
Thumbnail image of graphical abstract

Fluorine, the other hydrogen: Fluorinated forms of histidine, namely 2- and 4-fluorohistidines (see scheme), have dramatically reduced side-chain pKa's compared to the native amino acid. Biosynthetic incorporation of these analogues into bacterially expressed proteins should, therefore, broaden studies that are aimed at understanding pH- dependent processes. In this study we apply this technique to the production of fluorinated PapD chaperone.

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