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 basic principles of protein folding and activity. The presence of a natural
scaling region ending at an approximate threshold 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.
Keywords: Albumin; Allosteric effect; Assortativity; Bioinformatics; Computational biochemistry; Contact order; DBA; Degree based assortativity; Graph theory; Long-range interaction networks; Long-range order; Protein contact network; Structural biology; Topological invariants; aminoacids; hemoglobin flexibility
Document Type: Research Article
Publication date: 01 October 2012
- Current Proteomics research in the emerging field of proteomics is growing at an extremely rapid rate. The principal aim of Current Proteomics is to publish well-timed review articles in this fast-expanding area on topics relevant and significant to the development of proteomics. Current Proteomics is an essential journal for everyone involved in proteomics and related fields in both academia and industry.
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