Detalle de: Review: Conformation and Folding of Novel Beta-Structural Elements in Viral Fiber Proteins: The Triple Beta-Spiral and Triple Beta-Helix
| Title | Review: Conformation and Folding of Novel Beta-Structural Elements in Viral Fiber Proteins: The Triple Beta-Spiral and Triple Beta-Helix |
| Abstract |
Apart from alpha-helical coiled coils and the collagen triple helices, fibrous proteins can contain beta-structure in various conformations. Elongated enzymes such as pectate lyase and the bacteriophage P22 tailspike protein contain single-stranded beta-helices. Virus and bacteriophage fibers, which are often trimeric, have been shown to contain novel triple-stranded beta-structures such as the triple beta-spiral and the triple beta-helix. The conformation and folding of viral fibers containing beta-structure are discussed. |
| Apa Reference | Mitraki, A., Miller, S., & van Raaij, M. J. (2002). Review: Conformation and Folding of Novel Beta-Structural Elements in Viral Fiber Proteins: The Triple Beta-Spiral and Triple Beta-Helix. Journal of Structural Biology, 137(1–2), 236–247. 10.1006/jsbi.2002.4447 |
| Doi | 10.1006/jsbi.2002.4447 |
| Publication Date | Jan 2002 |
| Publication Type | Article |
| Researcher | Mark van Raaij |
| Ontology | Viromics |
| Research Groups | Structural Biology of Virus Proteins |
| Tools |
