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Ann M. Woys, Ph.D.

Affiliations: 
2012 Chemistry University of Wisconsin, Madison, Madison, WI 
Area:
2D IR spectroscopy
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"Ann Woys"
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Martin T. Zanni grad student 2012 UW Madison
 (Developing two-dimensional IR spectroscopy as a quantitative probe for protein structure.)

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Publications

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Woys AM, Briggs JL. (2016) Simple method for monitoring protein secondary structure during thermal unfolding and aggregation Spectroscopy (Santa Monica). 31: 47
Peran I, Oudenhoven T, Woys AM, et al. (2014) General strategy for the bioorthogonal incorporation of strongly absorbing, solvation-sensitive infrared probes into proteins. The Journal of Physical Chemistry. B. 118: 7946-53
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
Woys AM, Mukherjee SS, Skoff DR, et al. (2013) A strongly absorbing class of non-natural labels for probing protein electrostatics and solvation with FTIR and 2D IR spectroscopies. The Journal of Physical Chemistry. B. 117: 5009-18
Woys AM, Almeida AM, Wang L, et al. (2012) Parallel β-sheet vibrational couplings revealed by 2D IR spectroscopy of an isotopically labeled macrocycle: quantitative benchmark for the interpretation of amyloid and protein infrared spectra. Journal of the American Chemical Society. 134: 19118-28
Middleton CT, Marek P, Cao P, et al. (2012) Two-dimensional infrared spectroscopy reveals the complex behaviour of an amyloid fibril inhibitor. Nature Chemistry. 4: 355-60
Moran SD, Woys AM, Buchanan LE, et al. (2012) Two-dimensional IR spectroscopy and segmental 13C labeling reveals the domain structure of human γD-crystallin amyloid fibrils. Proceedings of the National Academy of Sciences of the United States of America. 109: 3329-34
Wang L, Middleton CT, Singh S, et al. (2011) 2DIR spectroscopy of human amylin fibrils reflects stable β-sheet structure. Journal of the American Chemical Society. 133: 16062-71
Marek P, Woys AM, Sutton K, et al. (2010) Efficient microwave-assisted synthesis of human islet amyloid polypeptide designed to facilitate the specific incorporation of labeled amino acids. Organic Letters. 12: 4848-51
Middleton CT, Woys AM, Mukherjee SS, et al. (2010) Residue-specific structural kinetics of proteins through the union of isotope labeling, mid-IR pulse shaping, and coherent 2D IR spectroscopy. Methods (San Diego, Calif.). 52: 12-22
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