Approach for comparing protein structures and origami models

Hay Azulay, Aviv Lutaty, Nir Qvit

Research output: Contribution to journalArticlepeer-review


The research fields of proteins and origami have intersected in the study of folding and de-novo design of proteins. However, there is limited knowledge on the analogy between protein structures and origami models. We propose a general approach for comparing protein structures with origami models, and present a test case, comparing transmembrane β-barrel and α-helical barrel with the Yoshimura and Kresling origami models. While both shapes and structures may look similar, we demonstrated that the β-barrel and the α-helical barrel are in agreement only with the shape and structural characteristics of the Kresling model. Through the analogy, it is explained how the structural characteristic can help the β-barrel and α-helical barrel to adjust length and diameter in response to changes in the membrane structure. However, such conformations only apply to the α-helical barrel, and the β-barrel, in spite of resembles to the Kresling model, remains stiff due to hydrogen bonds between the β-strands. Thus, our analysis suggests that there are similar patterns between protein structures and origami models and that the proposed approach may provide important insight on the role that the structure of a protein fulfils, and on the preferred structural design of novel proteins with unique characteristics.

Original languageEnglish
Article number183132
JournalBiochimica et Biophysica Acta - Biomembranes
Issue number2
StatePublished - 1 Feb 2020


  • Kresling model
  • Origami
  • Protein
  • Structure
  • Yoshimura model
  • α-Helical barrel
  • β-Barrel

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Cell Biology


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