1. Effect of Fluoro-Amino Acids on Protein Secondary Structure Stability
Richard Cheng, Department of Chemistry, University at Buffalo, SUNY
Buffalo, NY
The stability of enzymes catalysts for application in organic synthesis can be improved by incorporating fluorinated amino acids. We aim to measure the -helix and -sheet propensities of fluoro-amino acids. This would be useful for quantitatively predicting the effect of fluoro-amino acids on protein stability. We have measured the helix propensity (in both monomeric helices and dimeric coiled coils of fluoro-amino acids such as Hfl, showing that helix propensity decreases significantly upon introducing fluorines. We have also measured the sheet propensity of fluoro-amino acids such as Hfl, showing that sheet propensity increases upon introducing fluorines. This suggests that fluoro-amino acids such as Hfl may be more suitable for stabilizing -sheet structures compared to -helices to realize the full potential of the fluoro-stabilization effect.