Abstract

Systematic exchange of amino acid residues of similar physicochemical properties maintains specific coiled-coil interaction between two heptad repeats of HIV-1 gp41, as well as the biological activity of related peptide fusion inhibitors. This exchangeability can greatly degenerate sequence space of peptides thus making ab initio design of coiled-coil interaction feasible.

Full Text
Published version (Free)

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call