Effect of Highly Fluorinated Amino Acids on Protein Stability at a Solvent-Exposed Position on an Internal Strand of Protein G B1 Domain

摘要

Highly fluorinated amino acids can stabilize proteins for potential application in various protein biotechnologies including therapeutics and biosensors. Pioneering work to enhance protein stability by substituting natural hydrocarbon amino acids with fluoro-amino acids has mostly focused on helical proteins. However, the helicity of monomeric Ala-based peptides decreases upon replacing hydrocarbon amino acids with the corresponding fluorocarbon amino acids, suggesting that fluoro-amino acids may be more suitable for nonhelical secondary structures such as β-sheets.