Elsa Yan, PhD
Professor of ChemistryCards
About
Titles
Professor of Chemistry
Admission Committee Chair, Chemistry; Review Panelist, Molecular Architecture of Life
Positions outside Yale
Editorial Board Members, Biophysical Journal, Biophysical Society; Scientific Advisory Board Members, Polymer Research, Max Planck Institute
Biography
Elsa Yan was born and grew up in Hong Kong. She graduated from the Chinese University of Hong Kong in 1995. Working with Kenneth Eisenthal on nonlinear optics and surface sciences, she obtained her Ph.D. at Columbia University in 2000. From 2000-2004, she was a postdoctoral fellow in Richard Mathies's lab at UC Berkeley and a visiting fellow in Thomas Sakmar's lab at the Rockefeller University. She combined Raman spectroscopy with techniques in molecular biology to understand the molecular mechanism of signal transduction in the G-protein coupled receptor rhodopsin. In 2004, she joined The Rockefeller University, where she continued to develop methods in expression and purification of membrane proteins. In 2007, Elsa became an Assistant Professor of Chemistry at Yale. She was promoted to Associate Professor in 2012 and Full Professor in 2014.
Appointments
Chemistry
ProfessorPrimary
Other Departments & Organizations
- Biochemistry, Quantitative Biology, Biophysics and Structural Biology (BQBS)
- Center for RNA Science and Medicine
- Chemistry
- Yale Combined Program in the Biological and Biomedical Sciences (BBS)
Education & Training
- Postdoctoral Fellow
- Rockefeller University (2007)
- Postdoctoral Fellow
- University of California, Berkeley (2004)
- PhD
- Columbia University, Chemistry (2000)
- BS
- Chinese University of Hong Kong, Chemistry (1995)
Research
Overview
(1) Amyloid Aggregation on Cell membrane
The misfolding of amyloid proteins on cell membrane is associated with the onset of amyloid diseases. However, the investigation is challenging due to a lack of methods that allows direct observation of changes in protein secondary structures on membrane surfaces without using molecular labels. We develop a surface-specific vibrational spectroscopic method, chiral sum frequency generation. The method has enabled us to observe in situ and in real time the misfolding of amyloid proteins from disordered structures to ?lpha-helices and then beta-sheets on membrane surface. The results provide insight into the pathogenic mechanism and rational drug design.
(2) GPCR Signal Transduction across Cell Membrane
Seven-alpha-helical transmembrane G protein-coupled receptors (GPCRs) belong to the largest gene family in the human genome and represent important drug targets. We use nanodiscs to purify GPCRs and unnatural amino acid mutagenesis to site-specifically label GPCRs. Then, we exploit methods in biophysical spectroscopy to obtain highly selective spectroscopic readouts to report conformational changes of GPCRs during activation. The results will reveal the activation mechanism of GPCRs at the molecular level, guiding rational drug design targeting GPCRs.
(3) Transmembrane Visual Pigments in Molecular Mechanism of Vision
GPCR rhodopsin is a very sensitive biological light detector with extremely low dark noise. We aim to understand the molecular basis of its low dark noise level. The results will provide a strong basis to understand inherited eye diseases caused by mutations in the rhodopsin gene leading to retinitis pigmentosa, a family of progressive retinal degenerative diseases. The studies will also provide insight into molecular evolution of vertebrate vision, revealing the molecular mechanism in the divergence of cone pigments to rod pigments in the development of vertebrate dim-light vision.