Does secondary structure determine tertiary structure in proteins?

Haipeng Gong, George D. Rose

Research output: Contribution to journalArticlepeer-review


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° × 60° 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.

Original languageEnglish (US)
Pages (from-to)338-343
Number of pages6
JournalProteins: Structure, Function and Genetics
Issue number2
StatePublished - Nov 1 2005

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Biology


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