Abstract
The three-dimensional structure of a protein can be described as a graph where nodes represent residues and interactions between them are edges. We have constructed protein contact networks at different length-scales for different interaction strength cutoffs. The largest connected component of short-range networks exhibit a highly cooperative transition, while long- and all-range networks (more similar to each other), have less cooperativity. The hydrophobic subnetworks in all- and long-range networks have similar phase transition behaviours while hydrophilic and charged networks don’t. Hydrophobic subclusters in long- and all-range networks exhibit higher occurrence of assortativity and hence higher communication ability in transmitting information within a protein. The highly cliquish hydrophobic nodes in long- and short-range networks play a significant role in bridging and stabilizing distantly placed residues during protein folding. We have also observed a significant dominance of charged residues cliques in short-range networks.
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Sengupta, D., Kundu, S. (2012). Role of Physico-chemical Properties of Amino Acids in Protein’s Structural Organization: A Network Perspective. In: Lones, M.A., Smith, S.L., Teichmann, S., Naef, F., Walker, J.A., Trefzer, M.A. (eds) Information Processign in Cells and Tissues. IPCAT 2012. Lecture Notes in Computer Science, vol 7223. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-28792-3_11
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DOI: https://doi.org/10.1007/978-3-642-28792-3_11
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