Structural and Functional Analysis of Hemoglobin and Serum Albumin Through Protein Long-Range Interaction Networks

Long-range contacts in protein structures were demonstrated to be predictive of different physiological properties of hemoglobin and albumin proteins. Complex networks based approach was demonstrated to highlight ba- sic principles of protein folding and activity. The presence of a natural scaling region ending at an approximate thresh- old of 120-150 residues shared by proteins of different size and quaternary structure was highlighted. This threshold is reminiscent of the typical size for a macromolecule to have a binding site sensible to environmental regulation.

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