Approach for comparing protein structures and origami models
| Autor: | Hay Azulay, Nir Qvit, Aviv Lutaty |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
Physics
0303 health sciences Protein Folding Biophysics Membrane structure A protein 02 engineering and technology Cell Biology Molecular Dynamics Simulation Biochemistry Transmembrane protein Folding (chemistry) 03 medical and health sciences Barrel 020303 mechanical engineering & transports Protein structure 0203 mechanical engineering Protein Domains Sequence Analysis Protein Biological system Algorithms 030304 developmental biology Bacterial Outer Membrane Proteins |
| Zdroj: | Biochimica et biophysica acta. Biomembranes. 1862(2) |
| ISSN: | 1879-2642 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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