Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Magda Drewniak-Świtalska"'
Autor:
Ewa Rudzińska-Szostak, Paweł Morawiak, Łukasz Berlicki, Magda Drewniak-Świtalska, Barbara Barycza
Publikováno v:
Organic & Biomolecular Chemistry. 19:4272-4278
The construction of β-amino acid-containing peptides that fold to tertiary structures in solution remains challenging. Two model miniproteins, namely, Trp-cage and FSD, were scanned using a constrained β-amino acid in order to evaluate its impact o
Autor:
Monika Szefczyk, Katarzyna Ożga, Magda Drewniak-Świtalska, Ewa Rudzińska-Szostak, Rafał Hołubowicz, Andrzej Ożyhar, Łukasz Berlicki
Publikováno v:
RSC advances. 12(8)
The key issue in the research on foldamers remains the understanding of the relationship between the monomers structure and conformational properties at the oligomer level. In peptidomimetic foldamers, the main goal of which is to mimic the structure
Autor:
Jacek Plewka, Paulina Fortuna, Wojciech Rypniewski, Magda Drewniak-Świtalska, Magdalena Bejger, Łukasz Berlicki
Publikováno v:
Chemical communications (Cambridge, England). 57(49)
A new miniprotein built from three helices, including one structure based on the ααβαααβ sequence pattern was developed. Its crystal structure revealed a compact conformation with a well-packed hydrophobic core of unprecedented structure. The
Publikováno v:
ChemPlusChem. 86(4)
Numerous beta-amino acid containing peptides forming secondary structures have been already described, however the design of higher-order structures remains poorly explored. The methodology allowing construction of sequence patterns containing few ri
Autor:
Krzysztof Wycisk, Magda Drewniak-Świtalska, Łukasz Berlicki, Marek Orłowski, Aneta Tarczewska, Andrzej Ożyhar, Jurek Dobrucki, Agnieszka Waligórska
The FKBP39 from Drosophila melanogaster is a multifunctional regulatory immunophilin. It contains two globular domains linked by a highly charged disordered region. The N-terminal domain shows homology to the nucleoplasmin core domain, and the C-term
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::00c7a9d842fade95baaa1089568f3e34
https://ruj.uj.edu.pl/xmlui/handle/item/265987
https://ruj.uj.edu.pl/xmlui/handle/item/265987