Mutations in the tailspike gene (gene 9) of Salmonella typhimurium pha
ge P22 have been used to identify amino acid interactions during the f
olding of a polypeptide chain. Since temperature-sensitive folding (ts
f) mutations cause folding defects in the P22 tailspike polypeptide ch
ain, it is likely that mutants derived from these and correcting the o
riginal tsf defects (second-site intragenic suppressors) identify inte
ractions during the folding pathway. We report the isolation and ident
ification of second-site revertants to tsf mutants.