The exo-chirality of the α-helix and its implications in peptide self-assembly
The alpha-helix has an unexplored potential to draw a second layer of chirality encoded in the order of the primary sequence. In this thesis, we have empirically and computationally demonstrated the existence of exo-helical architectures arising from the first six periodic repetition patterns i, i +...
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| Tipo de recurso: | tesis doctoral |
| Fecha de publicación: | 2025 |
| País: | España |
| Institución: | Universidad de Santiago de Compostela (USC) |
| Repositorio: | Minerva. Repositorio Institucional de la Universidad de Santiago de Compostela |
| Idioma: | inglés |
| OAI Identifier: | oai:dnet:minerva_____::f4e03dd559d89f8b740d356b234d7655 |
| Acceso en línea: | https://hdl.handle.net/10347/41594 |
| Access Level: | acceso abierto |
| Palabra clave: | Peptide alpha-helix chirality coiled coil circular dichroism 230418 Polipéptidos y proteínas |
| Sumario: | The alpha-helix has an unexplored potential to draw a second layer of chirality encoded in the order of the primary sequence. In this thesis, we have empirically and computationally demonstrated the existence of exo-helical architectures arising from the first six periodic repetition patterns i, i +x, x = 2-7 in the sequence. A systematic study using a non-canonical chromophore residue with different spacer lengths revealed that a high exo-helix consistency is required to induce ordered coiled coils. Finally, we have also demonstrated for the first time that non-canonical exo-helical patterns can build coiled-coil structures. This study offers a novel perspective in the design of protein-based materials with promising structural and functional features. |
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