Yu-Shan Lin | |
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Alma mater | |
Scientific career | |
Fields | Computational Chemistry |
Institutions | Tufts University |
Doctoral advisor | James L. Skinner |
Other academic advisors | Vijay S. Pande (postdoctoral) |
Website | https://ase.tufts.edu/chemistry/lin/index.html |
Yu-Shan Lin is a computational chemist. She is a professor and chair of the Department of Chemistry at Tufts University in the United States. [1] Her research lab uses computational chemistry to understand and design biomolecules, with topics focusing on cyclic peptides, [2] [3] protein folding, [4] [5] and collagen. [6] [7]
Lin received her BS in chemistry from National Taiwan University in 2004. [8] Lin received her PhD in chemistry in 2009 from University of Wisconsin, Madison, under the guidance of James L. Skinner. [9] She then moved to Stanford, where she was a Bio-X postdoctoral fellow in the lab of Vijay S. Pande. [10] In 2012, Lin joined the Department of Chemistry at Tufts University and received tenure in 2018. [8] In 2024, Lin was appointed to a full professorship and became chair of the department. [11]
Lin and her lab use computational chemistry to provide information on the solution structures of cyclic peptides. [2] They recently successfully used molecular dynamics simulation with enhanced sampling methods to design well-structured cyclic peptides. [12] [13]
Lin and her lab are interested in understanding how co- and post-translational modifications and non-natural amino acids impact protein folding. [14] [15] They also work on understanding the effects of amino acid substitutions during evolution on protein stability, folding, and interaction. [16] [17]
Lin and her lab use molecular dynamics simulations to understand how the structure, stability, and interactions of collagen are perturbed by Gly to Ser substitutions, a very common type of Gly missense mutations in patients with Osteogenesis Imperfecta (OI), [18] [19] [20] and Ser phosphorylation. [21] Their results suggest a new possible mechanism underlying OI pathology, specifically that mutations may significantly disrupt the triple-helical structure of collagen and render it susceptible to non-collagenase proteolytic enzymes. [19]
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