We predict  that diagonal correlations of amino acid positions within protein sequences statistically enhance protein propensity for promiscuous 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 potential and the average amino acid composition. We suggest experimental and bioinformatics approaches to test ] the predicted effect.
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 URLanismal proteomes J. Mol. Biol. 409, 439 (2011)]. We suggest experiments that will allow direct testing of the predicted effect.
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analytically
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promiscuous binding.
nonspecific binding. We use the term 'promiscuity' to describe such nonspecific binding.
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potential
potentials
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We suggest experimental and bioinformatics approaches to test
Our analytical results provide an explanation for the enhanced diagonal correlations observed in hubs of URLanismal proteomes
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J. Mol. Biol. 409, 439 (2011)
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. We suggest experiments that will allow direct testing of