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Raman spectroscopic study on the conformation of 11 S form acetylcholinesterase from Torpedo californica

  • Dimitrina Aslanian
  • , Pál Gróf
  • , Michel Négrerie
  • , Minko Balkanski
  • , Palmer Taylor
  • Sorbonne Université
  • Department of Pharmacology

Research output: Contribution to journalArticlepeer-review

Abstract

Vibrational Raman spectroscopy has been used to study the conformation of the 11 S form of acetylcholine-sterase from Torpedo californica. Secondary structure analysis by the method of Williams [(1983) J. Mol. Biol. 166, 581-603] shows 49% α-helical structure, 23% β-sheets, 11% turns and 15% undefined structure. Secondary structure estimates obtained for this enzyme by Raman spectroscopy and circular dichroism have been analyzed.

Original languageEnglish
Pages (from-to)202-206
Number of pages5
JournalFEBS Letters
Volume219
Issue number1
DOIs
Publication statusPublished - 13 Jul 1987

Keywords

  • Acetylcholinesterase
  • Raman spectroscopy
  • Secondary structure

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