Emily B. Dunkelberger, Ph.D. - Publications
Affiliations: | 2013 | Chemistry | University of Wisconsin, Madison, Madison, WI |
Area:
2D IR spectroscopyYear | Citation | Score | |||
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2018 | Buchanan LE, Maj M, Dunkelberger EB, Cheng PN, Nowick JS, Zanni MT. Structural polymorphs suggest competing pathways for the formation of amyloid fibrils that diverge from a common intermediate species. Biochemistry. PMID 30375231 DOI: 10.1021/Acs.Biochem.8B00997 | 0.663 | |||
2015 | Dunkelberger EB, Grechko M, Zanni MT. 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. PMID 26446575 DOI: 10.1021/Acs.Jpcb.5B07706 | 0.696 | |||
2013 | Buchanan LE, Dunkelberger EB, Tran HQ, Cheng PN, Chiu CC, Cao P, Raleigh DP, de Pablo JJ, Nowick JS, Zanni MT. 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. PMID 24218609 DOI: 10.1073/Pnas.1314481110 | 0.712 | |||
2013 | Dunkelberger EB, Woys AM, Zanni MT. 2D IR cross peaks reveal hydrogen-deuterium exchange with single residue specificity. The Journal of Physical Chemistry. B. 117: 15297-305. PMID 23659731 DOI: 10.1021/Jp402942S | 0.674 | |||
2012 | Dunkelberger EB, Buchanan LE, Marek P, Cao P, Raleigh DP, Zanni MT. Deamidation accelerates amyloid formation and alters amylin fiber structure. Journal of the American Chemical Society. 134: 12658-67. PMID 22734583 DOI: 10.1021/Ja3039486 | 0.705 | |||
2011 | Middleton CT, Buchanan LE, Dunkelberger EB, Zanni MT. Utilizing Lifetimes to Suppress Random Coil Features in 2D IR Spectra of Peptides. The Journal of Physical Chemistry Letters. 2: 2357-2361. PMID 21966585 DOI: 10.1021/Jz201024M | 0.71 | |||
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