title: Phage tailspike protein. A fishy tale of protein folding.
abstract: The crystal structure of bacteriophage P22 tailspike protein reveals a striking fold with a distinctive, fish-like appearance, and helps explain many of the properties of this unusual molecule and its folding pathway.
authors.affiliation: Department of Biology, University of Utah, Salt Lake City 84112.
authors.forename: D P
authors.initials: DP
authors.lastname: Goldenberg
authors.forename: T E
authors.initials: TE
authors.lastname: Creighton
mesh_terms: D017100:Bacteriophage P22 / Q000737:chemistry* / Q000235:genetics / Q000648:ultrastructure; D003460:Crystallization; D005814:Genes, Viral; D006026:Glycoside Hydrolases / Q000737:chemistry* / Q000235:genetics; D008958:Models, Molecular; D009154:Mutation; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D014764:Viral Proteins / Q000737:chemistry* / Q000235:genetics; D017376:Viral Tail Proteins
chemical_list: D014764:Viral Proteins; D017376:Viral Tail Proteins; D006026:Glycoside Hydrolases; C083268:tailspike protein, bacteriophage