Curvature sensing of curvature-inducing proteins with internal structure
| Autor: | Noguchi, Hiroshi |
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| Rok vydání: | 2023 |
| Předmět: | |
| Zdroj: | Phys. Rev. E 109, 024403 (2024) |
| Druh dokumentu: | Working Paper |
| DOI: | 10.1103/PhysRevE.109.024403 |
| Popis: | Many types of peripheral and transmembrane proteins can sense and generate membrane curvature. Laterally isotropic proteins and crescent proteins with twofold rotational symmetry, such as Bin/Amphiphysin/Rvs superfamily proteins, have been studied theoretically. However, proteins often have an asymmetric structure or a higher rotational symmetry. We theoretically studied the curvature sensing of proteins with asymmetric structures and structural deformations. First, we examined proteins consisting of two rod-like segments. When proteins have mirror symmetry, their sensing ability is similar to that of single-rod proteins; hence, with increasing protein density on a cylindrical membrane tube, a second- or first-order transition occurs at a middle or small tube radius, respectively. As asymmetry is introduced, this transition becomes a continuous change, and metastable states appear at high protein densities. Protein with threefold, fivefold, or higher rotational symmetry has laterally isotropic bending energy. However, when a structural deformation is allowed, the protein can have a preferred orientation and stronger curvature sensing. Comment: 10 pages, 11 figures |
| Databáze: | arXiv |
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