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Intermolecular interactions between chloroplast lipids and a polypeptide fraction from thylakoids were investigated by far ultraviolet circular dichroism. The polypeptide fraction was isolated from dodecyl sulfate-containing buffers. It exhibits an average molecular weight of 24 000. The circular dichroism of this polypeptide fraction measured as mean residue ellipticity is greater in the presence of sodium dodecyl sulfate than in the absence of this detergent. This effect is reversible. Addition of sulfoquinovosyl diglyceride to the dodecyl sulfate-free solution of the polypeptide also causes an increase of the circular dichroism. This increase was only observed in the pH-range between 6.9 and 7.4. The effect of dodecyl sulfate or sulfolipid on the circular dichroism is interpreted to indicate an increase of α-helix content. Monogalactosyl diglyceride, digalactosyl di­glyceride and phosphatidyl glycerol gave no reaction. The attempt to obtain a conformational analysis of the polypeptide in the different states did not yield an entirely satisfactory result. Antisera to sulfolipid inhibit photosynthetic electron transport of stroma-freed chloroplasts in the region of light reaction I. This inhibition is restricted to the same pH-range as the non-covalent binding of sulfolipid to the polypeptides. It appears that in the cell membrane-bound metabolic processes are regulated by this pH-dependence of the sulfolipid-polypetide interactions.

Intermolecular Interactions of Polypeptides and Lipids in the Thylakoid Membrane