Investigating the tolerance of coiled-coil peptides to nonheptad sequence inserts.

@article{Hicks2002InvestigatingTT,
  title={Investigating the tolerance of coiled-coil peptides to nonheptad sequence inserts.},
  author={Matthew R. Hicks and John Walshaw and Derek N. Woolfson},
  journal={Journal of structural biology},
  year={2002},
  volume={137 1-2},
  pages={73-81}
}
Coiled-coil motifs foster a wide variety of protein-protein interactions. Canonical coiled coils are based on 7-residue repeats, which guide the folding and assembly of amphipathic alpha-helices. In many cases such repeats remain unbroken for tens to hundreds of residues. However, the sequences of an increasing number of putative and characterised coiled coils digress from this pattern. We probed the consequences of nonheptad inserts using a designed leucine-zipper system. The parent peptide… CONTINUE READING

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