Emily B. Dunkelberger, Ph.D.

2013 Chemistry University of Wisconsin, Madison, Madison, WI 
2D IR spectroscopy
"Emily Dunkelberger"
Mean distance: 9.56


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Martin T. Zanni grad student 2013 UW Madison
 (Using Two-Dimensional Infrared Spectroscopy as a Tool for Studying Amyloid and Membrane Proteins.)
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Buchanan LE, Maj M, Dunkelberger EB, et al. (2018) Structural polymorphs suggest competing pathways for the formation of amyloid fibrils that diverge from a common intermediate species. Biochemistry
Dunkelberger EB, Grechko M, Zanni MT. (2015) Transition Dipoles from 1D and 2D Infrared Spectroscopy Help Reveal the Secondary Structures of Proteins: Application to Amyloids. The Journal of Physical Chemistry. B. 119: 14065-75
Buchanan LE, Dunkelberger EB, Tran HQ, et al. (2013) Mechanism of IAPP amyloid fibril formation involves an intermediate with a transient β-sheet. Proceedings of the National Academy of Sciences of the United States of America. 110: 19285-90
Dunkelberger EB, Woys AM, Zanni MT. (2013) 2D IR cross peaks reveal hydrogen-deuterium exchange with single residue specificity. The Journal of Physical Chemistry. B. 117: 15297-305
Dunkelberger EB, Buchanan LE, Marek P, et al. (2012) Deamidation accelerates amyloid formation and alters amylin fiber structure. Journal of the American Chemical Society. 134: 12658-67
Middleton CT, Buchanan LE, Dunkelberger EB, et al. (2011) Utilizing Lifetimes to Suppress Random Coil Features in 2D IR Spectra of Peptides. The Journal of Physical Chemistry Letters. 2: 2357-2361
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