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

FEBS Letters

Négrerie, Michel¹  Balkanski, Minko¹  Taylor, Palmer²  Aslanian, Dimitrina¹  Gróf, Pál¹ 

[1] Laboratoire de Physique des Solides, Associé au CNRS, Université Pierre et Marie Curie, 4, Place Jussieu, 75230 Paris Cedex 05, France;Department of Pharmacology, University of California, San Diego, La Jolla, CA 92093, USA

关键词: Raman spectroscopy;    Acetylcholinesterase;    Secondary structure;   

DOI  :  10.1016/0014-5793(87)81216-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown