Abstract
In order to test a suggestion that inositol may take the place of water in maintaining the stability of desiccated cells, the reversible endothermic association of tobacco mosaic virus protein (TMVP) was studied turbidimetrically in presence of this substance. Its effect was to lower the temperature at which association takes place, the positive standard enthalpy and standard entropy of reaction both being increased by about 30%. The hypothesis of direct substitution of bound water by inositol at the site of macromolecular association leads to the contrary prediction that the association temperature would be raised. It is suggested that the observed effect of inositol may result from a conformation change in TMVP brought about by binding of inositol at positions adjacent to the site of reaction.
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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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