Fluorinated amino acids in protein design and engineering
Chemical Society Reviews2002Vol. 31(6), pp. 335–341
Citations Over TimeTop 10% of 2002 papers
Abstract
Selective incorporation of unnatural amino acids into proteins is a powerful tool for illuminating the principles of protein design. In particular, fluorinated amino acids have recently emerged as valuable building blocks for designing hyperstable protein folds, as well as directing highly specific protein-protein interactions. We review the collagen mimetic and coiled coil peptide systems that exemplify generalizable paradigms for future design. The unique electronic and phase properties of fluorocarbons are discussed, and protein synthesis using unnatural amino acids is briefly reviewed.
Related Papers
- → Rational design of enzyme activity and enantioselectivity(2023)120 cited
- → Rational-Design Engineering to Improve Enzyme Thermostability(2021)25 cited
- → Rational design of TNFα binding proteins based on the de novo designed protein DS119(2016)7 cited
- → Rational Design of Protein Cages for Alternative Enzymatic Functions(2013)6 cited
- → Protein Structure Design and Engineering(2011)3 cited