Franco O. Tzul, Ph.D.

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2009 Chemistry University of Montana, Missoula, MT 
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"Franco Tzul"
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Bruce Bowler grad student 2009 Univ. Montana
 (Thermodynamics and kinetics of iso-1-cytochrome c denatured state.)
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Publications

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Tzul FO, Vasilchuk D, Makhatadze GI. (2017) Reply to Candel et al.: Evidence for evolutionary conservation of folding kinetics in the thioredoxin protein family. Proceedings of the National Academy of Sciences of the United States of America
Tzul FO, Vasilchuk D, Makhatadze GI. (2017) Evidence for the principle of minimal frustration in the evolution of protein folding landscapes. Proceedings of the National Academy of Sciences of the United States of America
Srivastava KR, French KC, Tzul FO, et al. (2016) Intramolecular diffusion controls aggregation of the PAPf39 peptide. Biophysical Chemistry. 216: 37-43
Tzul FO, Schweiker KL, Makhatadze GI. (2015) Modulation of folding energy landscape by charge-charge interactions: linking experiments with computational modeling. Proceedings of the National Academy of Sciences of the United States of America. 112: E259-66
Tzul FO, Schweiker KL, Makhatadze GI. (2015) Modulation of folding energy landscape by charge-charge interactions:Linking experiments with computational modeling Proceedings of the National Academy of Sciences of the United States of America. 112: E259-E266
Wafer LN, Tzul FO, Pandharipande PP, et al. (2014) Structural and thermodynamic characterization of the recognition of the S100-binding peptides TRTK12 and p53 by calmodulin. Protein Science : a Publication of the Protein Society. 23: 1247-61
Wafer LN, Tzul FO, Pandharipande PP, et al. (2013) Novel interactions of the TRTK12 peptide with S100 protein family members: specificity and thermodynamic characterization. Biochemistry. 52: 5844-56
Makhatadze G, Tzul F, Schweiker K. (2013) Effect of Ionizable Residues on the Folding Energy Landscape of Globular Proteins: Linking Experiment and Computation Biophysical Journal. 104: 189a
Patel MM, Tzul F, Makhatadze GI. (2011) Equilibrium and kinetic studies of protein cooperativity using urea-induced folding/unfolding of a Ubq-UIM fusion protein. Biophysical Chemistry. 159: 58-65
Tzul FO, Bowler BE. (2010) Denatured states of low-complexity polypeptide sequences differ dramatically from those of foldable sequences. Proceedings of the National Academy of Sciences of the United States of America. 107: 11364-9
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