Items where Author is "Jaremko, Łukasz"

Article

Jaremko, Łukasz and Jaremko, Mariusz and Ejchart, Andrzej and Nowakowski, Michał (2018) Fast evaluation of protein dynamics from deficient 15N relaxation data. Journal of Biomolecular NMR, 70 (4). pp. 219-228. ISSN 0925-2738

Jaremko, Łukasz and Jaremko, Mariusz and Nowakowski, Michał and Ejchart, Andrzej (2015) The Quest for Simplicity: Remarks on the Free-Approach Models. Journal of Physical Chemistry B, 2015 (119). pp. 11978-11987. ISSN 1520-6106

Jaremko, Mariusz and Jaremko, Łukasz and Nowakowski, Michał and Wojciechowski, Marek and Szczepanowski, Roman H. and Panecka, Renata and Zhukov, Igor and Bochtler, Matthias and Ejchart, Andrzej (2014) NMR structural studies of the first catalytic half-domain of ubiquitin activating enzyme. Journal of Structural Biology, 185 (1). pp. 69-78. ISSN 1047-8477

Nowakowski, Michał and Ruszczyńska-Bartnik, Katarzyna and Budzińska, Monika and Jaremko, Łukasz and Jaremko, Mariusz and Zdanowski, Konrad and Bierzyński, Andrzej and Ejchart, Andrzej (2013) Impact of calcium binding and thionylation of S100A1 protein on its NMR derived structure and backbone dynamics. Biochemistry, 52 (7). pp. 1149-1159. ISSN Print Edition ISSN: 0006-2960

Nowakowski, Michał and Jaremko, Łukasz and Jaremko, Mariusz and Zhukov, Igor and Belczyk, Agnieszka and Bierzyński, Andrzej and Ejchart, Andrzej (2011) Solution NMR structure and dynamics of human apo-S100A1 protein. Journal of Structural Biology, 174 (2). pp. 391-399. ISSN 1047-8477

Jaremko, Mariusz and Jaremko, Łukasz and Lisowski, Marek and Makowski, M (2010) Effect of the ΔPhe residue configuration on a didehydropeptides conformation: A combined CD and NMR study. Effect of the ΔPhe residue configuration on a didehydropeptides conformation: A combined CD and NMR study .

Jaremko, Łukasz and Jaremko, Mariusz and Giachin, G and Legname, G (2010) NMR structure of the human prion protein with the pathological Q212P mutation reveals unique structural features. NMR structure of the human prion protein with the pathological Q212P mutation reveals unique structural features. .