Abstract
We previously prepared the de novo designed peptide, [YGG(IEKKIEA)4], which forms a parallel triple-stranded coiled coil. To prepare an AAB-type heterotrimeric α-helical bundle, two variants, where the Ile15 residue in the hydrophobic position was replaced with either an Ala or Trp residue, were designed and named IZ-2A and IZ-2W, respectively. Circular dichroism spectroscopy, peptide titration, sedimentation equilibrium, and gel filtration analyses revealed the formation of an (IZ-2A)2/IZ-2W complex. The NOESY spectra analyses indicated the presence of interstrand interactions between the two Ala residues and the Trp residue in the hydrophobic core. The (IZ-2A)2/IZ-2W complex has the structural uniqueness of native proteins.
Original language | English |
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Pages (from-to) | 212-215 |
Number of pages | 4 |
Journal | Journal of the American Chemical Society |
Volume | 122 |
Issue number | 2 |
DOIs | |
Publication status | Published - Jan 19 2000 |
Externally published | Yes |
All Science Journal Classification (ASJC) codes
- Catalysis
- Chemistry(all)
- Biochemistry
- Colloid and Surface Chemistry