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Sara Sohail


Assistant Professor of Chemistry

Chemistry & Biochemistry-Chemistry


  2. Phone: (610) 328-8561
  3. Science Center 186
Sara Sohail
B.S. Chemistry, Haverford College
Ph.D. Chemistry, University of Chicago
Nancy Nossal Postdoctoral Fellow, Laboratory of Chemical Physics (NIDDK/NIH)
Chem 042 (Physical Chemistry I)
Chem 052 (Physical Chemistry II)
Recent Publications
*undergraduate co-author
SH Sohail, S Sohoni, PC Ting, LR Fantz*, S. Abdulhadi, A Hitchcock, C MacGregor-Chatwin, CN Hunter, GS Engel, SC Massey. A photoprotective mechanism involving red chlorophylls of cyanobacterial photosystem I (submitted to Chemical Science)
JS Higgins, MA Allodi, LT Lloyd, JP Otto, SH Sohail, RG Saer, RE Wood, SC Massey, PC Ting, RE Blankenship, GS Engel. Redox conditions correlated with vibronic coupling modulate quantum beats in photosynthetic pigment-protein complexes. Proc. Natl. Acad. Sci., 118(49) (2021), e2112817118.
JS Higgins, LT Lloyd, SH Sohail, MA Allodi, JP Otto, RG Saer, RE Wood, SC Massey, PC Ting, RE Blankenship, GS Engel. Photosynthesis tunes quantum mechanical mixing of electronic and vibrational states to steer exciton energy transfer. Proc. Natl. Acad. Sci., 118(11) (2021), e2018240118.
SH Sohail, JP Otto, PD Cunningham, RE Wood, JS Higgins, MA Allodi, JS Melinger, GS Engel. DNA scaffold supports long-lived vibronic coherence in an indodicarbocyanine (Cy5) dimer. Chem. Sci. 11 (32), 8546-8557 (2020).
SC Massey, S-H Yeh, PC Ting, PD Dahlberg, SH Sohail, MA Allodi, EC Martin, S Kais, CN Hunter, GS Engel. Orientational Dynamics of Transition Dipoles and Exciton Relaxation in LH2 from Ultrafast Two-Dimensional Anisotropy. J. Phys. Chem. Lett 10, 270-277 (2019).
MA Allodi, JP Otto, SH Sohail, RG Saer, RE Wood, BS Rolczynski, SC Massey, PC Ting, RE Blankenship, GS Engel. Redox Conditions Affect Ultrafast Exciton Transport in Photosynthetic Pigment–Protein Complexes. J. Phys. Chem. Lett. 9 (1), 89-95 (2017).
SH Sohail, PD Dahlberg, MA Allodi, SC Massey, PC Ting, EC Martin, CN Hunter, GS Engel. Communication: Broad manifold of excitonic states in light-harvesting complex 1 promotes efficient unidirectional energy transfer in vivo. J. Chem. Phys. 147 (13), 131101 (2017).

Our research seeks to understand the physical mechanisms of amyloid fibril assembly. While amyloids are most publicly prominent due to their connection to devastating neurodegenerative diseases, amyloids are found as functional assemblies in all classes of life, representing a highly stable, thermodynamically favorable conformation of nearly any polypeptide. Amyloids are mechanically strong, robust to degradation, and bio-compatible, making them an attractive design scaffold for nano-biomaterials. Although amyloid fibril formation is a highly specific self-assembly process, fibrillation pathways are highly dependent on solution conditions. Mixtures of fibrils with unique morphologies and physicochemical properties are often co-present within the same sample. Our research group will characterize amyloid polymorphism using Fluorescence Lifetime Imaging Microscopy (FLIM), assessing polymorphic distributions from the single fibril level. We will use different solution conditions to evaluate the driving forces of polymorphic amyloid assembly for both functional and disease-related amyloids, gaining physical insight into protein self-assembly and how to better control it for biomaterial applications.