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. 1981 Aug;68(2):447–452. doi: 10.1104/pp.68.2.447

Noncovalent Intermolecular Forces in Phycobilisomes of Porphyridium cruentum1,2

Barbara A Zilinskas 1, Richard E Glick 1
PMCID: PMC427508  PMID: 16661934

Abstract

Using sensitized fluorescence as a measure of intactness of phycobilisomes isolated from Porphyridium cruentum, the effects of various environmental perturbations on phycobilisome integrity were investigated. The rate of phycobilisome dissociation in 0.75 ionic strength sodium salts proceeds in the order: SCN− > NO3− > Cl− > C6H5O73− > SO42− > PO43−, as predicted from the lyotropic series of anions and their effects on hydrophobic interactions in proteins. Similarly, increasing temperature (to 30 C) and pH values approaching the isoelectric points of the biliproteins stabilize phycobilisomes. Deuterium substitution at exchangeable sites on the phycobiliproteins decreases the rate of phycobilisome dissociation, while substitution at nonexchangeable sites increases rates of dissociation. It is concluded that hydrophobic intermolecular interactions are the most important forces in maintaining the phycobilisome structure. Dispersion forces also seem to contribute to phycobilisome stabilization. The adverse effects of electrostatic repulsion must not be ignored; however, it seems that the requirement of phycobilisomes of high salt concentrations is not simply countershielding of charges on the proteins.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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