PMID: 7372409Feb 1, 1980Paper

Predictor for sulfur-aromatic interactions in globular proteins

International Journal of Peptide and Protein Research
R S Morgan, J M McAdon

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.

References

Mar 1, 1978·International Journal of Peptide and Protein Research·R S MorganP K Warme
Jan 25, 1978·Journal of Molecular Biology·P K Warme, R S Morgan

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Citations

Aug 23, 2016·Nature Chemical Biology·Andrew K LewisJonathan N Sachs
Jan 1, 1987·International Journal of Peptide and Protein Research·M LeblV J Hruby
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