Optimizing the Fold Stability of Miniprotein Sequences
Peptides (< 25 residues) rarely have well-defined, deep energy wells for folding with the possible exception of a reported few hairpin and miniprotein structures. However, these systems display relatively low melting temperatures and broad thermal transitions for unfolding. Our lab has recently employed several strategies that provide exceptional stability for both types of folds.
KeywordsCircular Dichroism Cyclic Peptide Circular Dichroism Data Backbone Torsion Backbone Torsion Angle
The work was funded by an NIH grant (GM050658) to N. H. Andersen.