A tail of protein folding.
This review describes the use of a simple genetic system that has provided important insight into the process of folding and, of its flipside, that of protein aggregation. These studies make use of the tail protein of the bacterial virus P22 which infects Salmonella typhimurium. This folding system serves as a model for a number protein structural elements and may also provide important insights into disease-related protein folding defects at a time when an increasing number of diseases are being shown to be due to protein folding alterations.
Villafañe
R J
RJ
Department of Microbiology & Immunology, Universidad Central del Caribe School of Medicine, Bayamón, Puerto Rico 00960-6032. drbob@uccaribe.edu
Baksi
K
K
D000596:Amino Acids / Q000235:genetics / Q000378:metabolism; D017100:Bacteriophage P22 / Q000235:genetics* / Q000502:physiology; D004279:DNA, Viral / Q000235:genetics; D006801:Humans; D006868:Hydrolysis; D066298:In Vitro Techniques; D009154:Mutation; D011487:Protein Conformation; D017510:Protein Folding; D012486:Salmonella typhimurium / Q000821:virology; D017376:Viral Tail Proteins / Q000235:genetics*
D000596:Amino Acids; D004279:DNA, Viral; D017376:Viral Tail Proteins