Sean D. Moran
Associate Professor
Phone: 618-453-6545
Fax: 618-453-6408
smoran@chem.siu.edu
Use of infrared (2D IR) spectroscopy, protein semisynthesis and site-specific labeling techniques to:
1. Examine the structures and physical properties of β-sheet rich biological materials and use this information in biomaterials design.
2. Investigate the functional roles of fast (fs-ps) vibrational dynamics in the functions of photoactive proteins, electron transfer proteins and enzymes.
Education
B.Sc., McGill University
Ph.D., Columbia University
Postdoc, University of Wisconsin-Madison and Oberlin College; University of Wisconsin-Madison
Awards
NSF-GK12 Teaching Fellowship 2004-2006, Columbia University, New York, NY
Jack Miller Award 2004, Columbia University, New York, NY
James McGill Award 2000, McGill University, Montreal, Quebec
John W. Hooper Scholarship 2000, McGill University, Montreal, Quebec
Selected Publications
Moran , S.D.and Zanni, M.T. How to get Insights into Amyloid Structure and Formation from Infrared Spectroscopy Invited Perspective Article to J. Phys. Chem. Lett. 2014, 5, 1984-1993.
Buchanan, L.E.; Carr, J.K.; Fluitt, A.M.; Hoganson, A.J.; Moran, S.D.; DePablo, J.J.; Skinner, J.L.; Zanni, M.T. Structure motif of polyglutamine amyloid fibrils discerned with mixed-isotope infrared spectroscopy Proc. Natl. Acad. Sci. U.S.A., 2014, 111, 5796-5801.
Moran, S.D.; Zhang, T.O.; Zanni, M.T. An alternative structural isoform in amyloid-like aggregates formed from thermally denatured human γD-crystallin Protein Science 2014, 23, 321-331.
Lam, A.; Moran, S.D.; Preketes, N.; Zhang, T.O.; Zanni, M.T.; Mukamel, S.Study of the γD- Crystallin Protein Using Two-dimensional Infrared (2D IR) Spectroscopy: Experiment and Simulation, J. Phys. Chem. B. 2013, 117, 15436-15443.
Moran, S.D.; Zhang, T.; Decatur, S.M.; Zanni, M.T. Amyloid Fiber Formation in Human γD- crystallin Induced by UV-B Photodamage, Biochemistry 2013, 52, 6169-6181.
Woys, A.M.; Mukherjee, S. Skoff, D.R.; Moran, S.D.; Zanni, M.T. A Strongly Absorbing Class of Non-Natural Labels for Probing Protein Electrostatics and Solvation with FTIR and 2D IR Spectroscopies, J.Phys. Chem. B. 2013, 117, 5009-5018.
Moran, S.D.; Decatur, S.M.; Zanni, M.T. Structural and Sequence Analysis of the Human γD- Crystallin Amyloid Fibril Core Using 2D IR spectroscopy, Segmental 13C Labeling, and Mass Spectrometry, J. Am. Chem. Soc., 2012, 134, 18410-18416.
Moran, S.D.; Woys, A.M.; Buchanan, L.E.; Bixby, E.; Decatur, S.M.; Zanni, M.T. Two-Dimensional IR Spectroscopy and Segmental 13C Labeling Reveals the Domain Structure of Human γD-Crystallin Amyloid Fibrils, Proc. Natl. Acad. Sci. U. S. A., 2012, 109(9), 3329-3334.
This work was highlighted in C&E News (SciCon, Vol. 90, Issue 7, p. 37)
Westerlund, K.; Moran, S.D.; Privett, H.K.; Hay, S.; Jarvet, J.; Gibney, B.R.; Tommos, C. Making a Single-Chain Four-Helix Bundle For Redox Chemistry Studies, Protein Engineering , Design, and Selection, 2008, 21, 645-652.