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Peter Silinski, Ph.D.

Affiliations: 
2003 Duke University, Durham, NC 
Area:
protein folding and stability
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"Peter Silinski"
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Michael C. Fitzgerald grad student 2003 Duke
 (Understanding the role of backbone -backbone hydrogen bonding in the folding and stability of the hexameric enzyme 4-oxalocrotonate tautomerase (4OT).)

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Cisneros GA, Wang M, Silinski P, et al. (2006) Theoretical and experimental determination on two substrates turned over by 4-oxalocrotonate tautomerase. The Journal of Physical Chemistry. A. 110: 700-8
Cisneros GA, Wang M, Silinski P, et al. (2004) The protein backbone makes important contributions to 4-oxalocrotonate tautomerase enzyme catalysis: understanding from theory and experiment. Biochemistry. 43: 6885-92
Silinski P, Fitzgerald MC. (2003) Comparative analysis of two different amide-to-ester bond mutations in the beta-sheet of 4-oxalocrotonate tautomerase. Biochemistry. 42: 6620-30
Powell KD, Wang MZ, Silinski P, et al. (2003) The accuracy and precision of a new H/D exchange- and mass spectrometry-based technique for measuring the thermodynamic stability of proteins Analytica Chimica Acta. 496: 225-232
Silinski P, Fitzgerald MC. (2002) A stable dimer in the pH-induced equilibrium unfolding of the homo-hexameric enzyme 4-oxalocrotonate tautomerase (4-OT). Biochemistry. 41: 4480-91
Moss JA, Silinski P, Fitzgerald MC. (2001) Mapping tertiary interactions in protein folding reactions: a novel mass spectrometry- and chemical synthesis-based approach. Fresenius' Journal of Analytical Chemistry. 369: 252-7
Silinski P, Allingham MJ, Fitzgerald MC. (2001) Guanidine-induced equilibrium unfolding of a homo-hexameric enzyme 4-oxalocrotonate tautomerase (4-OT). Biochemistry. 40: 4493-502
Nakhle BM, Silinski P, Fitzgerald MC. (2000) Identification of an essential backbone amide bond in the folding and stability of a multimeric enzyme Journal of the American Chemical Society. 122: X
Nakhle BM, Silinski P, Fitzgerald MC. (2000) Identification of an essential backbone amide bond in the folding and stability of a multimeric enzyme Journal of the American Chemical Society. 122: X
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