Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Grzegorz Ścibisz"'
Autor:
Michał Kluz, Hanna Nieznańska, Robert Dec, Igor Dzięcielewski, Bartosz Niżyński, Grzegorz Ścibisz, Wojciech Puławski, Grzegorz Staszczak, Ewelina Klein, Julita Smalc-Koziorowska, Wojciech Dzwolak
Publikováno v:
PLoS ONE, Vol 14, Iss 6, p e0218975 (2019)
Bovine serum albumin (BSA) is often employed as a proteinaceous component for synthesis of luminescent protein-stabilized gold nanoclusters (AuNC): intriguing systems with many potential applications. Typically, the formation of BSA-AuNC conjugate oc
Externí odkaz:
https://doaj.org/article/cc0ade19bd0242b4b42b65d915dd99d3
Publikováno v:
PLoS ONE, Vol 12, Iss 10, p e0187328 (2017)
Due to its symmetric structure and abundance of carboxyl groups, mellitic acid (MA-benzenehexacarboxylic acid) has an uncommon capacity to form highly ordered molecular networks. Dissolved in water, MA dissociates to yield various mellitate anions wi
Externí odkaz:
https://doaj.org/article/3f146ae4b3d5453fbc0ee46f011a4a6f
Autor:
Mateusz Fortunka, Marcin Guza, Matylda Wacławska, Robert Dec, Wojciech Puławski, Grzegorz Ścibisz, Wojciech Dzwolak
Publikováno v:
The journal of physical chemistry. B. 123(43)
Conformational transitions involving aggregated proteins or peptides are of paramount biomedical and biotechnological importance. Here, we report an unusual freeze-induced structural reorganization within a β-sheet-rich ionic coaggregate of poly(l-l
Autor:
Grzegorz Staszczak, Grzegorz Ścibisz, Ewelina Klein, Robert Dec, Igor Dzięcielewski, Wojciech Puławski, Julita Smalc-Koziorowska, Wojciech Dzwolak, Bartosz Niżyński, Michał Kluz, Hanna Nieznanska
Publikováno v:
PLoS ONE, Vol 14, Iss 6, p e0218975 (2019)
PLoS ONE
PLoS ONE
Bovine serum albumin (BSA) is often employed as a proteinaceous component for synthesis of luminescent protein-stabilized gold nanoclusters (AuNC): intriguing systems with many potential applications. Typically, the formation of BSA-AuNC conjugate oc
Autor:
Sylwia, Berbeć, Robert, Dec, Dmitry, Molodenskiy, Beata, Wielgus-Kutrowska, Christian, Johannessen, Agnieszka, Hernik-Magoń, Fernando, Tobias, Agnieszka, Bzowska, Grzegorz, Ścibisz, Timothy A, Keiderling, Dmitri, Svergun, Wojciech, Dzwolak
Publikováno v:
The journal of physical chemistry. B. 122(50)
Replacing water with dimethyl sulfoxide (DMSO) completely reshapes the free-energy landscapes of solvated proteins. In DMSO, a powerful hydrogen-bond (HB) acceptor, formation of HBs between backbone NH groups and solvent is favored over HBs involving
Publikováno v:
PLoS ONE, Vol 12, Iss 10, p e0187328 (2017)
PLoS ONE
PLoS ONE
Due to its symmetric structure and abundance of carboxyl groups, mellitic acid (MA–benzenehexacarboxylic acid) has an uncommon capacity to form highly ordered molecular networks. Dissolved in water, MA dissociates to yield various mellitate anions
Autor:
Agnieszka Hernik-Magoń, Sylwia Berbeć, Dmitri I. Svergun, Christian Johannessen, Robert Dec, Agnieszka Bzowska, Fernando Tobias, Timothy A. Keiderling, Wojciech Dzwolak, Grzegorz Ścibisz, Beata Wielgus-Kutrowska, Dmitry S. Molodenskiy
Publikováno v:
The Journal of Physical Chemistry B
The journal of physical chemistry : B : condensed matter, materials, surfaces, interfaces and biophysical
The journal of physical chemistry : B : condensed matter, materials, surfaces, interfaces and biophysical
Replacing water with dimethyl sulfoxide (DMSO) completely reshapes the free-energy landscapes of solvated proteins. In DMSO, a powerful hydrogen-bond (HB) acceptor, formation of HBs between backbone NH groups and solvent is favored over HBs involving