Determination of the secondary structure of epoxide hydrolase by Raman spectroscopy.
The secondary structure of microsomal epoxide hydrolase was determined by Raman spectroscopy and the effect of the membrane microenvironment studied. The ratios of the four secondary structure contents, alpha-helix: beta-strand:turn:undefined, were found to be 47:24:17:11 and 58:17:15:10 for the solubilized and the membrane-bound epoxide hydrolase, respectively. Based on the spectral analysis in the 2800-2900 cm-1 range, it was concluded that the protein studied produces the disordering effect on the lipid dimyristoylphosphatidylcholine bilayer at 16 degrees C.
Ivanov
Y D
YD
Institute of Biological and Medical Chemistry, Moscow, Russia.
Izotov
A A
AA
Rukavishnikov
I G
IG
Uvarov VYu
D000818:Animals; D004134:Dimyristoylphosphatidylcholine; D004851:Epoxide Hydrolases / Q000737:chemistry* / Q000494:pharmacology; D008051:Lipid Bilayers / Q000737:chemistry; D008433:Mathematics; D008861:Microsomes / Q000201:enzymology; D015394:Molecular Structure; D017433:Protein Structure, Secondary; D051381:Rats; D013059:Spectrum Analysis, Raman / Q000379:methods
D008051:Lipid Bilayers; D004851:Epoxide Hydrolases; D004134:Dimyristoylphosphatidylcholine