Dusan Petrovic
Affiliations: | Uppsala University, Uppsala, Uppsala län, Sweden |
Area:
computational enzymology, enzyme evolution, enzyme designGoogle:
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Publications
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Longo LM, Petrović D, Kamerlin SCL, et al. (2020) Short and simple sequences favored the emergence of N-helix phospho-ligand binding sites in the first enzymes. Proceedings of the National Academy of Sciences of the United States of America |
Liao Q, Kulkarni Y, Sengupta U, et al. (2018) Loop Motion in Triosephosphate Isomerase is not a Simple Open and Shut Case. Journal of the American Chemical Society |
Hong NS, Petrović D, Lee R, et al. (2018) The evolution of multiple active site configurations in a designed enzyme. Nature Communications. 9: 3900 |
Schulte M, Petrović D, Neudecker P, et al. (2018) Conformational Sampling of the Intrinsically Disordered C-Terminal Tail of DERA Is Important for Enzyme Catalysis. Acs Catalysis. 8: 3971-3984 |
Maršavelski A, Petrović D, Bauer P, et al. (2018) Empirical Valence Bond Simulations Suggest a Direct Hydride Transfer Mechanism for Human Diamine Oxidase. Acs Omega. 3: 3665-3674 |
Petrović D, Risso VA, Kamerlin SCL, et al. (2018) Conformational dynamics and enzyme evolution. Journal of the Royal Society, Interface. 15 |
Uluca B, Viennet T, Petrović D, et al. (2018) DNP-Enhanced MAS NMR: A Tool to Snapshot Conformational Ensembles of α-Synuclein in Different States. Biophysical Journal. 114: 1614-1623 |
Petrović D, Bokel A, Allan M, et al. (2018) Simulation-guided design of cytochrome P450 for chemo- and regioselective macrocyclic oxidation. Journal of Chemical Information and Modeling |
Petrović D, Szeler K, Kamerlin SCL. (2018) Challenges and advances in the computational modeling of biological phosphate hydrolysis. Chemical Communications (Cambridge, England) |
Maurer D, Enugala TR, Hamnevik E, et al. (2018) Stereo- and Regioselectivity in Catalyzed Transformation of a 1,2-Disubstituted Vicinal Diol and the Corresponding Diketone by Wild Type and Laboratory Evolved Alcohol Dehydrogenases Acs Catalysis. 8: 7526-7538 |