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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
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