Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Olga Szczepankiewicz"'
Publikováno v:
Langmuir
Nanoparticles interfere with protein amyloid formation. Catalysis of the process may occur due to increased local protein concentration and nucleation on the nanoparticle surface, whereas tight binding or a large particle/protein surface area may lea
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6cbdd2e7687d96d65fcc53367b299479
https://doi.org/10.1021/la203078w
https://doi.org/10.1021/la203078w
Publikováno v:
Proceedings of the National Academy of Sciences. 107:19826-19831
Protein stabilization was achieved through in vivo screening based on the thermodynamic linkage between protein folding and fragment complementation. The split GFP system was found suitable to derive protein variants with enhanced stability due to th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::328f1f2ce7bc6c7d72b0a5a17c1b50c6
https://doi.org/10.1073/pnas.1005689107
https://doi.org/10.1073/pnas.1005689107
Autor:
Birgitta Frohm, Michael T. Colvin, Olga Szczepankiewicz, Robert G. Griffin, Eva Thulin, Georg Meisl, Tuomas P. J. Knowles, Björn Linse, Angela C. Jacavone, Dominic M. Walsh, Sara Linse, Carlo Sala Frigerio
Amyloid β-protein (Aβ) sequence length variants with varying aggregation propensity coexist in vivo, where coaggregation and cross-catalysis phenomena may affect the aggregation process. Until recently, naturally occurring amyloid β-protein (Aβ)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0c7d26b483651fd2d646429ac5d73361
https://europepmc.org/articles/PMC5412961/
https://europepmc.org/articles/PMC5412961/
Publikováno v:
Journal of Molecular Biology. 358:1244-1255
The relative significance of weak non-covalent interactions in biological context has been much debated. Here, we have addressed the contribution of Coulombic interactions to protein stability and assembly experimentally. The sweet protein monellin,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f586fecfd1c18d5c1e38bdfc05dc8dad
https://doi.org/10.1016/j.jmb.2006.02.069
https://doi.org/10.1016/j.jmb.2006.02.069
Publikováno v:
Journal of Biological Chemistry. 277:41954-41959
Calbindin D(28k) (calbindin) is a member of the calmodulin superfamily of Ca(2+)-binding proteins. An intracellular target of calbindin was discovered using bacteriophage display. Human recombinant calbindin was immobilized on magnetic beads and used
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3f76542a10b6dae840a5515feda7b5bd
https://doi.org/10.1074/jbc.m203492200
https://doi.org/10.1074/jbc.m203492200
Autor:
Eva Thulin, Celia Cabaleiro-Lago, Michele Vendruscolo, Sara Linse, Olga Szczepankiewicz, Therese Hunter, Gian Gaetano Tartaglia, Hanna Nilsson, Gary J. Hunter
A series of recent studies have provided initial evidence about the role of specific intra-molecular interactions in maintaining proteins in their soluble state and in protecting them from aggregation. Here we show that the amino acid sequence of the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1295c0bd26c1fc090b2fbaa3222da177
http://hdl.handle.net/11573/1451778
http://hdl.handle.net/11573/1451778
Publikováno v:
Biochimica et biophysica acta. 1794(3)
A small number of proteins have the unusual property of tasting intensely sweet. Despite many studies aimed at identifying their sweet taste determinants, the molecular basis of protein sweetness is not fully understood. Recent mutational studies of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::030617d30dbeadf22b5e31f0ae667fda
https://pubmed.ncbi.nlm.nih.gov/19100868
https://pubmed.ncbi.nlm.nih.gov/19100868
Autor:
Hanna Nilsson, Mikael C. Bauer, Wei-Feng Xue, Sara Linse, Stina Lindman, Olga Szczepankiewicz
Publikováno v:
Biophysical Journal. (8):2911-2921
This study shows significant effects of protein surface charges on stability and these effects are not eliminated by salt screening. The stability for a variant of protein G B1 domain was studied in the pH-range of 1.5-11 at low, 0.15 M, and 2 M salt
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::33335279e14994fc1dd598fbfba0300c