Thomas C. Pochapsky
Affiliations: | Chemistry | Brandeis University, Waltham, MA, United States |
Area:
Physical Chemistry, BiochemistryWebsite:
http://www.bio.brandeis.edu/faculty/pochapsky.htmlGoogle:
"Thomas Pochapsky"Bio:
http://www.bio.brandeis.edu/pochapskylab/Pochapsky_Lab/People.html
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Publications
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Wong NR, Sundar R, Kazanis S, et al. (2023) Conformational heterogeneity suggests multiple substrate binding modes in CYP106A2. Journal of Inorganic Biochemistry. 241: 112129 |
Pochapsky TC. (2020) A dynamic understanding of cytochrome P450 structure and function through solution NMR. Current Opinion in Biotechnology. 69: 35-42 |
Pochapsky TC, Pochapsky SS. (2019) What Your Crystal Structure Will Not Tell You about Enzyme Function. Accounts of Chemical Research |
Wong NR, Liu X, Lloyd H, et al. (2018) A new approach to understanding structure-function relationships in cytochromes P450 by targeting terpene metabolism in the wild. Journal of Inorganic Biochemistry. 188: 96-101 |
Asciutto EK, Pochapsky TC. (2018) Some Surprising Implications of NMR-directed Simulations of Substrate Recognition and Binding by Cytochrome P450 (CYP101A1). Journal of Molecular Biology. 430: 1295-1310 |
Tietz DR, Colthart AM, Sondej Pochapsky S, et al. (2017) Substrate recognition by two different P450s: Evidence for conserved roles in a common fold. Scientific Reports. 7: 13581 |
Deshpande AR, Pochapsky TC, Ringe D. (2017) The Metal Drives the Chemistry: Dual Functions of Acireductone Dioxygenase. Chemical Reviews |
Tietz DR, Podust LM, Sherman DH, et al. (2017) Solution conformations and dynamics of substrate-bound cytochrome P450 MycG. Biochemistry |
Pochapsky TC, Wong N, Zhuang Y, et al. (2017) NADH reduction of nitroaromatics as a probe for residual ferric form high-spin in a cytochrome P450. Biochimica Et Biophysica Acta |
Deshpande AR, Pochapsky TC, Petsko GA, et al. (2017) Dual chemistry catalyzed by human acireductone dioxygenase. Protein Engineering, Design & Selection : Peds |