There's a right way and a wrong way: in vivo and in vitro folding, misfolding and subunit assembly of the P22 tailspike.
The in vivo and in vitro folding, assembly and misfolding of an elongated protein, the thermostable tailspike adhesin of phage P22, reveals important aspects of the sequence control of chain folding as well as its failure mode, inclusion body formation.
Department of Biology, Massachusetts Institute of Technology, Cambridge 02139, USA.
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Betts
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King
D017100:Bacteriophage P22 / Q000737:chemistry*; D002152:Calorimetry, Differential Scanning; D006026:Glycoside Hydrolases / Q000737:chemistry* / Q000235:genetics / Q000648:ultrastructure; D008854:Microscopy, Electron; D008958:Models, Molecular; D009154:Mutation; D011489:Protein Denaturation; D017510:Protein Folding; D017376:Viral Tail Proteins / Q000737:chemistry* / Q000235:genetics / Q000648:ultrastructure
D017376:Viral Tail Proteins; D006026:Glycoside Hydrolases; C083268:tailspike protein, bacteriophage