Matthias M. Waegele, Ph.D.

Affiliations: 
2011 University of Pennsylvania, Philadelphia, PA, United States 
Area:
Physical and Biological Chemistry
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"Matthias Waegele"
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Feng Gai grad student 2011 Penn
 (On the folding and conformation of peptides and the development of novel methods for their study.)
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Publications

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Waegele MM, Chen X, Herlihy DM, et al. (2014) How surface potential determines the kinetics of the first hole transfer of photocatalytic water oxidation. Journal of the American Chemical Society. 136: 10632-9
Waegele MM, Doan HQ, Cuk T. (2014) Long-lived photoexcited carrier dynamics of d - D excitations in spinel ordered Co3O4 Journal of Physical Chemistry C. 118: 3426-3432
Serrano AL, Waegele MM, Gai F. (2012) Spectroscopic studies of protein folding: linear and nonlinear methods. Protein Science : a Publication of the Protein Society. 21: 157-70
Waegele MM, Culik RM, Gai F. (2011) Site-Specific Spectroscopic Reporters of the Local Electric Field, Hydration, Structure, and Dynamics of Biomolecules. The Journal of Physical Chemistry Letters. 2: 2598-2609
Waegele MM, Gai F. (2011) Power-law dependence of the melting temperature of ubiquitin on the volume fraction of macromolecular crowders. The Journal of Chemical Physics. 134: 095104
Waegele MM, Gai F. (2010) Infrared study of the folding mechanism of a helical hairpin: porcine PYY. Biochemistry. 49: 7659-64
Waegele MM, Gai F. (2010) Computational Modeling of the Nitrile Stretching Vibration of 5-Cyanoindole in Water. The Journal of Physical Chemistry Letters. 1: 781-786
Montalvo G, Waegele MM, Shandler S, et al. (2010) Infrared signature and folding dynamics of a helical beta-peptide. Journal of the American Chemical Society. 132: 5616-8
Waegele MM, Tucker MJ, Gai F. (2009) 5-Cyanotryptophan as an Infrared Probe of Local Hydration Status of Proteins. Chemical Physics Letters. 478: 249-253
Mukherjee S, Waegele MM, Chowdhury P, et al. (2009) Effect of macromolecular crowding on protein folding dynamics at the secondary structure level. Journal of Molecular Biology. 393: 227-36
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