Identification of secondary structures in globular proteins ‐ a new algorithm*

C. Ramakrishna, K. V. Soman

Research output: Contribution to journalArticlepeer-review

46 Scopus citations


A new algorithm has been developed for identifying helices, extended structures, and bends from the positions of the α‐carbon atoms using the virtual bond approach. The parameters used are two virtual bond angles (Δ1 and Δ2), the virtual dihedral angle (θ), and the distance (D) between the terminal α‐carbon atoms of the tripeptide. The criteria for classification have been worked out by model building as well as from proteins whose complete secondary structures are known. These criteria are as follows: (i) |θ| ≤ 60° and (Δ12) ≤ 230° for a bend, (ii) for a helix, successive θ's should not differ by more than 30°, and (iii) for an extended structure, the cumulative deviation of the above parameters should not vary by more than 20% from the ideal extended chain. The method developed has been applied successfully to three proteins wherein the coordinates of α‐carbon atoms alone are known and a complete mapping of the secondary structures has now been obtained. One interesting observation is that the percentage of residues not taking part in helices, extended structures, and bends is very small ‐ of the order of 4%.

Original languageEnglish (US)
Pages (from-to)218-237
Number of pages20
JournalInternational Journal of Peptide and Protein Research
Issue number3
StatePublished - Sep 1982
Externally publishedYes


  • alpha helix
  • beta bend
  • conformational analysis
  • extended structure
  • globular protein
  • helices in proteins
  • secondary structure
  • virtual bond

ASJC Scopus subject areas

  • Biochemistry


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