  We predict analytically that diagonal correlations of amino acid positions
within protein sequences statistically enhance protein propensity for
nonspecific binding. We use the term 'promiscuity' to describe such nonspecific
binding. Diagonal correlations represent statistically significant repeats of
sequence patterns where amino acids of the same type are clustered together.
The predicted effect is qualitatively robust with respect to the form of the
microscopic interaction potentials and the average amino acid composition. Our
analytical results provide an explanation for the enhanced diagonal
correlations observed in hubs of eukaryotic organismal proteomes [J. Mol. Biol.
409, 439 (2011)]. We suggest experiments that will allow direct testing of the
predicted effect.
