PubMed · 7372409
Predictor for sulfur-aromatic interactions in globular proteins.
Abstract
The predictor, Y = 2.54 (formula: see text), where Y is the number of sulfur-aromatic interactions in a globular protein and N is the total number of amino acids in the protein, accounts for 75% of the variation in this type of interaction that occurs in 22 globular proteins whose three-dimensional structure has been determined. We find that S-pi interactions are not random events but rather are the outcome of a competition between the dipolar groups, amides and sulfur-containing, for ring neighbors. This outcome is strongly weighted in favor of S-pi interactions by the presence in the protein of positively charged side-chains; it is not affected by the number of strictly non-polar side-chains.
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R S Morgan, J M McAdon. 1980. Predictor for sulfur-aromatic interactions in globular proteins.. https://doi.org/10.1111/j.1399-3011.1980.tb02566.x
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