294-297<span style="font-size:12.0pt;font-family:
" times="" new="" roman";mso-fareast-font-family:"times="" roman";mso-ansi-language:="" en-in;mso-fareast-language:en-in;mso-bidi-language:ar-sa"="" lang="EN-IN">Three-dimensional
models of the chimeric S. typhi OmpC protein carrying an epitope from rotavirus
VP4 capsid protein on either of two exposed loops ( fourth and sixth) were
constructed separately, using computer-aided homology modelling. The theoretical
model of S. typhi OmpC was used as a template. The monomers were
initially energy minimized. The trimers were generated for both ihe chimeric S.
typhi OmpC proteins and the structures were optimized after several cycles
of minimization. The surface accessibility calculations for the resulting
models show that epitope recognition should be more effective in the fourth
loop than in the sixth loop. in accordance with the experimental results on the
immunogenic nature of the rotaviral epitope inserted into the two putative
loops of S. typhi OmpC.</span