Part of the Advances in Experimental Medicine and Biology book series (volume 611)
Quantitating Amino Acid β-Strand Preferences, Turn Propensities and Cross-Strand Interactions in a Designed Hairpin Peptide
Beta-hairpins have gained popularity in many research groups as simple models for β sheets. The present study focuses on optimizing β-hairpin peptide sequences, quantitating residue β propensities, and determining the energetic contributions from cross-strand interactions. Studies began with the 16-residue peptide (MrH4 = KKLTVSIXGKKITVSA). In our nomenclature the turn locus residues are designated as T1 and T2 with strand positions numbered S±# based on how far residues are before or after the turn site. The sites probed in the present study are the S±2 and S±4 strand sites and the T1and T2 turn sites. These are shown below.
KeywordsIndole Ring Energetic Contribution Backbone Chemical Shift Ring Current Effect Turn Propensity
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.
The work was funded by grants from the National Science Foundation.
© Springer Science+Business Media, LLC 2009