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Yu-Shan Lin

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This article is about the chemist. For the visual artist, see Lin Yushan.
Yu-Shan Lin
林郁珊
EducationNational Taiwan University (B.S., Chemistry)

University of Wisconsin, Madison (M.S. and Ph.D., Chemistry)

Stanford University (postdoctoral fellowship)
OccupationAssociate Professor of Chemistry at Tufts University
Awards
Websitehttps://ase.tufts.edu/chemistry/lin/index.html

Yu-Shan Lin is an Associate Professor 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] protein folding,[3] and collagen.[4][5]

Education

Lin received her B.S. in Chemistry from National Taiwan University in 2004.[6] Lin received her Ph.D. in Chemistry in 2009 from University of Wisconsin, Madison, under the guidance of Professor James L. Skinner. She then moved to Stanford, where she was a Bio-X postdoctoral fellow in the lab of Professor Vijay S. Pande.[7] In 2012, Lin joined the Department of Chemistry at Tufts University and received tenure in 2018.[6]

Research

Cyclic peptides

Lin and her lab aim to 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.[8][9]

Protein folding

Lin and her lab are interested in understanding how co- and post-translational modifications and non-natural amino acids impact protein folding.[10][11] They also work on understanding the effects of amino acid substitutions during evolution on protein stability, folding, and interaction.[12][13]

Collagen

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),[14][15][16] and Ser phosphorylation.[17] 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.[15]

Awards and honors

References

  1. ^ "Faculty | Department of Chemistry". chem.tufts.edu. Retrieved 2021-07-13.
  2. ^ a b Damjanovic, Jovan; Miao, Jiayuan; Huang, He; Lin, Yu-Shan (2021-02-24). "Elucidating Solution Structures of Cyclic Peptides Using Molecular Dynamics Simulations". Chemical Reviews. 121 (4): 2292–2324. doi:10.1021/acs.chemrev.0c01087. ISSN 0009-2665.
  3. ^ Mong, Surin K.; Cochran, Frank V.; Yu, Hongtao; Graziano, Zachary; Lin, Yu-Shan; Cochran, Jennifer R.; Pentelute, Bradley L. (2017-10-31). "Heterochiral Knottin Protein: Folding and Solution Structure". Biochemistry. 56 (43): 5720–5725. doi:10.1021/acs.biochem.7b00722. ISSN 0006-2960. PMC 5818992. PMID 28952732.
  4. ^ "Collagen interactions: Drug design and delivery". Advanced Drug Delivery Reviews. 97: 69–84. 2016-02-01. doi:10.1016/j.addr.2015.11.013. ISSN 0169-409X.
  5. ^ "Using synthetic peptides and recombinant collagen to understand DDR–collagen interactions". Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1866 (11): 118458. 2019-11-01. doi:10.1016/j.bbamcr.2019.03.005. ISSN 0167-4889.
  6. ^ a b "Yu-Shan Lin | YSL at Tufts". ase.tufts.edu. Retrieved 2021-07-13.
  7. ^ a b University, © Stanford; Stanford; California 94305 (2014-03-07). "Yu-Shan Lin - Bio-X Postdoctoral Fellow". Welcome to Bio-X. Retrieved 2021-07-11.{{cite web}}: CS1 maint: numeric names: authors list (link)
  8. ^ Slough, Diana P.; McHugh, Sean M.; Cummings, Ashleigh E.; Dai, Peng; Pentelute, Bradley L.; Kritzer, Joshua A.; Lin, Yu-Shan (2018-03-28). "Designing Well-Structured Cyclic Pentapeptides Based on Sequence–Structure Relationships". The Journal of Physical Chemistry B. 122 (14): 3908–3919. doi:10.1021/acs.jpcb.8b01747. ISSN 1520-6106. PMC 6071411. PMID 29589926.
  9. ^ Cummings, Ashleigh E.; Miao, Jiayuan; Slough, Diana P.; McHugh, Sean M.; Kritzer, Joshua A.; Lin, Yu-Shan (2019-02-05). "β-Branched Amino Acids Stabilize Specific Conformations of Cyclic Hexapeptides". Biophysical Journal. 116 (3): 433–444. doi:10.1016/j.bpj.2018.12.015. ISSN 0006-3495. PMID 30661666.
  10. ^ Rogers, Julia R.; McHugh, Sean M.; Lin, Yu-Shan (2017-09-27). "Predictions for α-Helical Glycopeptide Design from Structural Bioinformatics Analysis". Journal of Chemical Information and Modeling. 57 (10): 2598–2611. doi:10.1021/acs.jcim.7b00123. ISSN 1549-9596.
  11. ^ Simon, Mark D.; Maki, Yuta; Vinogradov, Alexander A.; Zhang, Chi; Yu, Hongtao; Lin, Yu-Shan; Kajihara, Yasuhiro; Pentelute, Bradley L. (2016-09-21). "d-Amino Acid Scan of Two Small Proteins". Journal of the American Chemical Society. 138 (37): 12099–12111. doi:10.1021/jacs.6b03765. ISSN 0002-7863.
  12. ^ Phillips, Angela M; Gonzalez, Luna O; Nekongo, Emmanuel E; Ponomarenko, Anna I; McHugh, Sean M; Butty, Vincent L; Levine, Stuart S; Lin, Yu-Shan; Mirny, Leonid A; Shoulders, Matthew D (2017-09-26). Palese, Peter (ed.). "Host proteostasis modulates influenza evolution". eLife. 6: e28652. doi:10.7554/eLife.28652. ISSN 2050-084X.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  13. ^ Phillips, Angela M.; Ponomarenko, Anna I.; Chen, Kenny; Ashenberg, Orr; Miao, Jiayuan; McHugh, Sean M.; Butty, Vincent L.; Whittaker, Charles A.; Moore, Christopher L.; Bloom, Jesse D.; Lin, Yu-Shan (2018-09-17). "Destabilized adaptive influenza variants critical for innate immune system escape are potentiated by host chaperones". PLOS Biology. 16 (9): e3000008. doi:10.1371/journal.pbio.3000008. ISSN 1545-7885. PMC 6160216. PMID 30222731.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  14. ^ Yigit, Sezin; Yu, Hongtao; An, Bo; Hamaia, Samir; Farndale, Richard W.; Kaplan, David L.; Lin, Yu-Shan; Brodsky, Barbara (2016-09-02). "Mapping the Effect of Gly Mutations in Collagen on α2β1 Integrin Binding *". Journal of Biological Chemistry. 291 (36): 19196–19207. doi:10.1074/jbc.M116.726182. ISSN 0021-9258. PMID 27432884.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  15. ^ a b Chhum, Panharith; Yu, Hongtao; An, Bo; Doyon, Brian R.; Lin, Yu-Shan; Brodsky, Barbara (2016-12-01). "Consequences of Glycine Mutations in the Fibronectin-binding Sequence of Collagen *". Journal of Biological Chemistry. 291 (53): 27073–27086. doi:10.1074/jbc.M116.753566. ISSN 0021-9258. PMID 27799304.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  16. ^ "Collagen Gly missense mutations: Effect of residue identity on collagen structure and integrin binding". Journal of Structural Biology. 203 (3): 255–262. 2018-09-01. doi:10.1016/j.jsb.2018.05.003. ISSN 1047-8477.
  17. ^ Qiu, Yimin; Poppleton, Erik; Mekkat, Arya; Yu, Hongtao; Banerjee, Sourav; Wiley, Sandra E.; Dixon, Jack E.; Kaplan, David L.; Lin, Yu-Shan; Brodsky, Barbara (2018-12-18). "Enzymatic Phosphorylation of Ser in a Type I Collagen Peptide". Biophysical Journal. 115 (12): 2327–2335. doi:10.1016/j.bpj.2018.11.012. ISSN 0006-3495. PMID 30527445.
  18. ^ "OpenEye Outstanding Junior Faculty Award in Computational Chemistry". www.acscomp.org. Retrieved 2021-07-11.
  19. ^ "Dreyfus Program for Machine Learning in the Chemical Sciences & Engineering Awards". Dreyfus Foundation. 2020-07-27. Retrieved 2021-07-11.
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