The proteolipid and its partially delipidated protein from brain tissue have been studied by optical rotatory dispersion and circular dichroism in various solvents. The protein exhibits a helix content of 60–70 per cent in chloroform‐methanol and 2‐chloroethanol and is dextrorotatory in the visible region. In 1,1,1‐trinuoroethanol, a higher helix content of 90 per cent is observed but the protein is laevorotatory. The helix content decreases in water and methanol with a much greater negative specific rotation in methanol. No random coil form has been observed.
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Sherman et al. (1970) studied this question.
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