Understanding the effects of post-translational modifications and non-natural amino acids on protein folding br> br> br>
Understanding protein folding has long been a research focus for chemists. Molecular dynamics simulations can provide atomistic-level information on protein structure and dynamics. However, the systems under investigation are usually small and “clean” — with no disulfide bond or modification.
In vivo, most proteins go through co-/post-translational modifications. One of the most common modifications is glycosylation. Glycans have crucial and diverse biological functions, modulating a wide variety of interactions. Besides these extrinsic effects, glycans can affect the intrinsic structure and stability of the glycoproteins. Glycosylation is often thought to induce or stabilize a beta-turn configuration on the attached proteins and we are working with a number of model peptides to characterize the origin and the strength of this induction and stabilization. From a protein engineering perspective, we are also very interested in the effects of non-natural amino acids on protein structure and folding.
M. D. Simon, Y. Maki, A. A. Vinogradov, C. Zhang, H. Yu, Y.-S. Lin, Y. Kajihara, B. L. Pentelute, “D-amino acid scan of two small proteins,” J. Am. Chem. Soc. 138, 12099 (2016).