Yu-Shan Lin
Tufts Chemistry


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Yu-Shan Lin
Department of Chemistry
Tufts University
62 Talbot Avenue Pearson 103-X
Medford, MA 02155

Email: yu-shan.lin@tufts.edu

Protein folding

Understanding the effects of post-translational modifications and non-natural amino acids on protein folding

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.

A. M. Phillips, L. O. Gonzalez, E. E. Nekongo, A. I. Ponomarenko, S. M. McHugh, V. Butty, S. S. Levine, Y.-S. Lin, L. A. Mirny, M. D. Shoulders, “Host proteostasis modulates influenza evolution,” eLife in press.

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, 12099‒12111 (2016).