Arbeidsområder
Ansvar for drift og vedlikehold av instrumenter (GC/FID, GC/MS) og opplæring i bruk av instrumentene.
Undervisning
FARM1150 - Farmasøytisk rettet biokjemi
FARM3100 - Farmakognosi
FARM5000 - Masterforberedende emne i farmasi
FARM5200 - Bruk av biopolymerer i legemidler og forbedring av helse
Bakgrunn
2015 - PhD i kjemi ved NMBU - “Thermodynamic aspects of processive enzymatic degradation of recalcitrant polysaccharides”
2010 - MSc i kjemi ved NMBU
2008 - BSc i bioteknologi ved NMBU
Publikasjoner
Hamre, A. G., Al-Sadawi, R., Johannesen, K. M., Bisarro, B., Kjendseth, Å. K., Leiros, H. K. S., and Sørlie M. (2023) Initial characterization of an iron-superoxide dismutase from Thermobifida fusca, J. Biol. Inorg. Chem. 28, 689-698.
Fu, Y., Malterud, K.E., Hamre, A. G., Inngjerdingen, K.T., and Wangensteen H. (2023) Polysaccharides and bioactive phenolics from Aconitum septentrionale roots, Chem. Biodiversity 20, e202300161.
Hamre, A.G. and Sørlie M. (2020) Kinetic relationships with processivity in Serratia marcescens family 18 glycoside hydrolases, Biochem. Biophys. Res. Commun. 521, 120-124.
Harmsen, R. A. G., Aam, B. B., Madhuprakash, J., Hamre, A. G., Goddard-Borger, E., Withers, S., Eijsink, V. G. H., and Sørlie M. (2020) Chemoenzymatic synthesis of chitooligosaccharides with alternating N-D-acetylglucosamine and D-glucosamine, Biochemistry 59, 4581-4590.
Hamre, A. G., Kaupang, A., Payne, C. M., Väljamäe, P., and Sørlie, M. (2019) Thermodynamic signatures of substrate binding for three Thermobifida fusca cellulases with different modes of action, Biochemistry 58, 1648-1659.
Hamre, A. G., Strømnes, A. G. S., Gustavsen, D. Vaaje-Kolstad, G., Eijsink V. G., and Sørlie, M. (2019) Treatment of recalcitrant crystalline polysaccharides with lytic polysaccharide monooxygenaserelieves the need for glycoside hydrolase processivity, Carbohydr. Res. 473, 66-71.
Jana, S., Hamre, A.G., Eijsink, V.G.H., Sørlie, M., and Payne, C.M. (2019) Polar residues lining the binding cleft of a Serratia marcescens family 18 chitinase position the substrate for attack and stabilize associative interactions, Mol. Phys. 117, 3664-3682.
Pechsrichuang, P., Lorentzen, S. B., Aam, B. B., Tuveng, T. R., Hamre, A.G., Eijsink, V. G., and Yamabhai, M. (2018) Bioconversion of chitosan into chito-oligosaccharides (CHOS) using family 46 chitosanase from Bacillus subtilis (BsCsn46A), Carbohydr. Polym. 186, 420-428.
Hamre, A. G., Frøberg, E. E., Eijsink, V.G., and Sørlie, M. (2017) Thermodynamics of tunnel formation upon substrate binding in a processive glycoside hydrolase, Arch. Biochem. Biophys., 620, 35-42.
Jana, S., Hamre, A. G., Wildberger, P., Holen, M. M., Eijsink, V. G., Beckham, G. T., Sørlie, M., and Payne, C. M. (2016) Aromatic-mediated carbohydrate recognition in processive Serratia marcescens chitinases, J. Phys. Chem. B. 120, 1236-1249.
Hamre, A. G., Jana, S., Reppert, N. K., Payne, C. M., and Sørlie, M. (2015) Processivity, substrate positioning, and binding: The role of polar residues in a family 18 glycoside hydrolase, Biochemistry 54, 7292-7306.
Hamre, A. G., Jana, S., Holen, M. M., Mathiesen, G., Väljamäe, P., Payne, C. M., and Sørlie, M. (2015) Thermodynamic relationships with processivity in Serratia marcescens family 18 chitinases, J. Phys. Chem. B, 119, 9601-9613.
Hamre, A. G., Schaupp, D., Eijsink, V. G., and Sørlie, M. (2015) The directionality of processive enzymes acting on recalcitrant polysaccharides is reflected in the kinetic signatures of oligomer degradation, FEBS Lett. 589, 1807-1812.
Hamre, A. G., Eide, K. B., Wold, H. H., and Sørlie, M. (2015) Activation of enzymatic chitin degradation by a lytic polysaccharide monooxygenase, Carbohydr. Res. 407, 166-169.
Hamre, A. G., Lorentzen, S. B., Väljamäe, P., and Sørlie, M. (2014) Enzyme processivity changes with the extent of recalcitrant polysaccharide degradation, FEBS Lett. 588, 4620-4624.
Kalayou, S., Hamre, A. G., Ndossi, D., Connolly, L., Sørlie, M., Ropstad, E., and Verhaegen, S. (2014) Using SILAC proteomics to investigate the effect of the mycotoxin, alternariol, in the human H295R steroidogenesis model, Cell Biol. Toxicol., 1-16.