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.
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