Villafañe R J, Baksi K
Department of Microbiology & Immunology, Universidad Central del Caribe School of Medicine, Bayamón, Puerto Rico 00960-6032.
P R Health Sci J. 1999 Jun;18(2):105-15.
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.