Determinants of fold stabilizing aromatic-aromatic interactions in short peptides
The significance of interactions involving aromatic side-chains in stabilizing protein structure is well accepted, while the geometry and specificity of these interactions are more elusive. Hydrophobic clustering plays a significant role; these interactions can be distinguished as aromatic/aliphatic and aromatic/aromatic interactions, with the aromatic/aromatic interactions displaying two dominant geometries — edge-to-face (EtF) and parallel displaced (PD) stacking .
KeywordsStrand Length Stabilize Protein Structure Flank Pair Parallel Displace Strand Peptide
The work was funded by NSF and NIH grants to Dr. Niels Andersen.