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Lin, Yi-Chih

Yi-Chih Lin

Assistant Professor
Department of Chemistry

Visualizing biomolecular dynamics in real-time and real-space


Office Location
WEL 3.226J

Postal Address
105 E 24TH ST
AUSTIN, TX 78712
  • B.S., in Chemistry - National Taiwan University (2007)
  • M.S., in Chemistry - National Taiwan University (2009)
  • Ph.D., in Chemistry - University of Pennsylvania (2017)
  • Postdoctoral Training in Anesthesiology, Biochemistry & Biophysics - Weill Cornell Medicine (2017-2021) 

In 2021, Yi-Chih joined the Department of Chemistry at the University of Texas at Austin. 

Research Interests

We develop High-Speed Atomic Force Microscopy (HS-AFM) and other biophysical tools to understand how the structural dynamics of biomolecules (lipids, peptides, proteins, nucleic acids) correlate to their physiological functions. Our current interests include understanding the structure-function correlation of membrane proteins in native-like environments, the properties of biological membranes, membrane-protein interactions, protein self-assembly and aggregation, and protein-nucleic acid interactions. To accomplish these goals, we directly visualize the structural and functional dynamics of biomolecules in real-time (10 frames per second), in real space (~1 angstrom in vertical, ~1 nm in the lateral resolution), in the physiological fluids, and under various environmental cues using HS-AFM.

Prospective students and postdocs are encouraged to reach out via e-mail.


  1. Lin, Y. C.*, Guo, Y. R.*, Miyagi, A., Levring, J., MacKinnon, R. & Scheuring, S. "Force-induced conformational changes in PIEZO1". Nature 573, 230-234, (2019). doi:10.1038/s41586-019-1499-2; https://www.ncbi.nlm.nih.gov/pubmed/31435018 *Equal contribution.
  2. Lin, Y. C., Chipot, C. & Scheuring, S. "Annexin-V stabilizes membrane defects by inducing lipid phase transition". Nat Commun 11, 230, (2020). doi:10.1038/s41467-019-14045-w; https://www.ncbi.nlm.nih.gov/pubmed/31932647
  3. Jiao, F., Cannon, K. S., Lin, Y. C., Gladfelter, A. S. & Scheuring. S. "The hierarchical assembly of septins revealed by high-speed AFM", Nat Commun 11, 5062, (2020). doi:10.1038/s41467-020-18778-x; https://pubmed.ncbi.nlm.nih.gov/33033254/
  4. Lin, Y. C., Skolnick, M. & Fakhraai, Z. "A Novel Method to Measure the Effective Change of the Interfacial Energy due to Kinetic Self-Assembly of Amyloid Fibrils". J Phys Chem B 123, 6990-6996, (2019). doi:10.1021/acs.jpcb.9b04717; https://www.ncbi.nlm.nih.gov/pubmed/31334647
  5. Lin, Y. C., Komatsu, H., Ma, J., Axelsen, P. H. & Fakhraai, Z. "Identifying Polymorphs of Amyloid-beta (1-40) Fibrils Using High-Resolution Atomic Force Microscopy". J Phys Chem B 123, 10376-10383, (2019). doi:10.1021/acs.jpcb.9b07854; https://www.ncbi.nlm.nih.gov/pubmed/31714085
  6. Lin, Y. C., Li, C. & Fakhraai, Z. "Kinetics of Surface-Mediated Fibrillization of Amyloid-beta (12-28) Peptides". Langmuir 34, 4665-4672, (2018). doi:10.1021/acs.langmuir.7b02744; https://www.ncbi.nlm.nih.gov/pubmed/29584444
  7. Lin, Y. C., Repollet-Pedrosa, M. H., Ferrie, J. J., Petersson, E. J. & Fakhraai, Z. "Potential Artifacts in Sample Preparation Methods Used for Imaging Amyloid Oligomers and Protofibrils due to Surface-Mediated Fibril Formation". J Phys Chem B 121, 2534-2542, (2017). doi:10.1021/acs.jpcb.6b12560; https://www.ncbi.nlm.nih.gov/pubmed/28266853
  8. Lin, Y. C., Komatsu, H., Ma, J. Q., Axelsen, P. H. & Fakhraai, Z. "Quantitative analysis of amyloid polymorphism using height histograms to correct for tip convolution effects in atomic force microscopy imaging". Rsc Advances 6, 114286-114295, (2016). doi:10.1039/c6ra24031c
  9. Lin, Y. C., Petersson, E. J. & Fakhraai, Z. "Surface effects mediate self-assembly of amyloid-beta peptides". ACS Nano 8, 10178-10186, (2014). doi:10.1021/nn5031669; https://www.ncbi.nlm.nih.gov/pubmed/25229233

The Lin group is an interdisciplinary team of biophysicists and biochemists. We develop high-speed atomic force microscopy (HS-AFM) with various toolkits and correlated microscopes to visualize biological processes at single-molecule level. We are especially interested in scientists that are at the interface of biophysics, biochemistry, and molecular biology. 


Applicants with a strong background in biophysics, molecular biology, biochemistry, biomedical engineering, instrumental designs, or computer science are strongly encouraged to apply. Please email Yi-Chih a CV and a cover letter that explains why you are interested in the lab.


Prospective graduate students that are interested in our research can join the lab by applying to the Chemistry PhD program.