We predict that multi-scale correlations of amino acid positions within protein sequences generically enhance protein propensity for promiscuous binding. We show that the enhanced sequence correlations are evolutionary selected URLanismal proteomes. We predict analytically the robustness of this biophysical effect with respect to the form of the interaction potential .
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 .
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multi-scale
diagonal
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generically
statistically
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We show that the enhanced sequence correlations are evolutionary selected URLanismal proteomes. We predict analytically the robustness of this biophysical effect
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
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interaction potential
microscopic interaction potential and the average amino acid composition. We suggest experimental and bioinformatics approaches to test the predicted effect