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• W2984223696 abstract "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." @default.
• W2984223696 created "2019-11-22" @default.
• W2984223696 creator A5001021574 @default.
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• W2984223696 date "2020-02-01" @default.
• W2984223696 modified "2023-09-27" @default.
• W2984223696 title "Approach for comparing protein structures and origami models" @default.
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• W2984223696 doi "https://doi.org/10.1016/j.bbamem.2019.183132" @default.
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