PubMed · 16104021
Does secondary structure determine tertiary structure in proteins?
Abstract
Is highly approximate knowledge of a protein's backbone structure sufficient to successfully identify its family, superfamily, and tertiary fold? To explore this question, backbone dihedral angles were extracted from the known three-dimensional structure of 2,439 proteins and mapped into 36 labeled, 60 degrees x 60 degrees bins, called mesostates. Using this coarse-grained mapping, protein conformation can be approximated by a linear sequence of mesostates. These linear strings can then be aligned and assessed by conventional sequence-comparison methods. We report that the mesostate sequence is sufficient to recognize a protein's family, superfamily, and fold with good fidelity.
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Haipeng Gong, George D Rose. 2005-11-01. Does secondary structure determine tertiary structure in proteins?. https://doi.org/10.1002/prot.20622
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