Abstract
Highly designable structures can be distinguished based on certain geometric graphical features of the interactions confirming the fact that the topology of a protein structure and its residue-residue interaction network are important determinants of its designability. The most designable structures and poorly designable structures obtained for sets of proteins having the same number of residues are compared, and it is shown that the most designable structures predicted by the graph features of the contact diagrams are more densely packed whereas the poorly designable structures are more open loop type structures or structures that are loosely packed. Interestingly enough, it can also be seen that these highly designable structures obtained are also common structural motifs found in nature.
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Leelananda, S.P., Jernigan, R.L., Kloczkowski, A. (2015). Exploration of Designability of Proteins Using Graph Features of Contact Maps: Beyond Lattice Models. In: Przytycka, T. (eds) Research in Computational Molecular Biology. RECOMB 2015. Lecture Notes in Computer Science(), vol 9029. Springer, Cham. https://doi.org/10.1007/978-3-319-16706-0_18
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DOI: https://doi.org/10.1007/978-3-319-16706-0_18
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