Kamil Szpotkowski
Polish Academy of Sciences
26 Papers
107 Citations
Kamil Szpotkowski is an academic researcher from Polish Academy of Sciences. The author has contributed to research in topics: Small-angle X-ray scattering & Plant protein. The author has an hindex of 8, co-authored 23 publications. Previous affiliations of Kamil Szpotkowski include Adam Mickiewicz University in Poznań.
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Papers
Structure of γ-conglutin: insight into the quaternary structure of 7S basic globulins from legumes.
Jaroslaw Czubinski,J. Barciszewski,Miroslaw Gilski,Kamil Szpotkowski,Janusz Debski,Eleonora Lampart-Szczapa,Mariusz Jaskolski +6 more
TL;DR: Structural elucidation of γ-conglutin will help to explain its physiological role, especially in the evolutionary context, and will guide further research into the hypoglycaemic activity of this protein in humans, with potential consequences for novel antidiabetic therapies.
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Structural characterization of a dimer of RNA duplexes composed of 8-bromoguanosine modified CGG trinucleotide repeats: a novel architecture of RNA quadruplexes
TL;DR: Evidence is provided for the existence of a novel quadruplex architecture comprising CGG repeats in the FMR1 gene, characterized using a variety of experimental methods, such as native gel electrophoresis, NMR spectroscopy, small-angle X-ray scattering and electrospray ionization mass spectrometry.
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Crystallographic and CD probing of ligand-induced conformational changes in a plant PR-10 protein.
Joanna Śliwiak,Rafał Dolot,Karolina Michalska,Kamil Szpotkowski,Grzegorz Bujacz,Michal M. Sikorski,Mariusz Jaskolski +6 more
TL;DR: The present work describes the first atomic models of the same PR-10 protein with and without a physiological ligand, which reveals that the conformation of LlPR-10.1A undergoes a significant structural rearrangement upon trans-zeatin binding.
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Self‐Assembly and Ordering of Peptide‐Based Cavitands in Water and DMSO: The Power of Hydrophobic Effects Combined with Neutral Hydrogen Bonds
Katarzyna Eichstaedt,Kamil Szpotkowski,Marcin Grajda,Miroslaw Gilski,Stanislaw Wosicki,Mariusz Jaskolski,Agnieszka Szumna +6 more
TL;DR: It is demonstrated that peptide-based cavitands wrap around a hydrophobic core by a combination of theHydrophobic effect and hydrogen-bonding interactions to form highly ordered three-component complexes in water that resemble the molten-globule stage of protein folding.
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The landscape of cytokinin binding by a plant nodulin
TL;DR: Four crystal structures of the MtN13 protein are reported in complexes with several cytokinins, namely trans-zeatin, N 6-isopentenyladenine, kinetin and N6-benzyladenin, which have excellent definition in the electron-density maps and appears to be strong and specific.
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