Raman spectroscopic study on the conformation of 11 S form acetylcholinesterase from Torpedo californica.
Vibrational Raman spectroscopy has been used to study the conformation of the 11 S form of acetylcholinesterase from Torpedo californica. Secondary structure analysis by the method of Williams [(1983) J. Mol. Biol. 166, 581-603] shows 49% alpha-helical structure, 23% beta-sheets, 11% turns and 15% undefined structure. Secondary structure estimates obtained for this enzyme by Raman spectroscopy and circular dichroism have been analyzed.
D000110:Acetylcholinesterase; D000577:Amides / Q000032:analysis; D000818:Animals; D002942:Circular Dichroism; D011487:Protein Conformation; D013059:Spectrum Analysis, Raman; D014101:Torpedo; D014364:Tryptophan / Q000032:analysis; D014443:Tyrosine / Q000032:analysis; D014961:X-Ray Diffraction
D000577:Amides; D014443:Tyrosine; D014364:Tryptophan; D000110:Acetylcholinesterase