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Determinants of fold stabilizing aromatic-aromatic interactions in short peptides

  • Lisa A. Eidenschink
  • Brandon L. Kier
  • Niels H. Andersen
Part of the Advances in Experimental Medicine and Biology book series (volume 611)

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 [1].

Cross-strand aryl/aryl pairings occur predominantly at non-H-bonded sites in P-sheets [ 2]. In p-hairpin models these have been found to be stabilizing at turn flanking positions [ 3]. The excised N-terminal hairpin of the B1 domain of Protein G has a Tyr/Phe pair at such a position and is required for hairpin formation [ 4]. Trpzip4 and its analogs display two EtF Trp/Trp interactions at non-H-bonded sites, the turn flanking pair accounts for the majority of stabilization. HP6 and HP7, two peptide series more remotely...

Keywords

Strand Length Stabilize Protein Structure Flank Pair Parallel Displace Strand Peptide 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Notes

Acknowledgments

The work was funded by NSF and NIH grants to Dr. Niels Andersen.

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Copyright information

© Springer Science+Business Media, LLC 2009

Authors and Affiliations

  • Lisa A. Eidenschink
    • 1
  • Brandon L. Kier
    • 1
  • Niels H. Andersen
    • 1
  1. 1.Department of ChemistryUniversity of WashingtonSeattleUSA

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