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The order of PDZ3 and TrpCage in fusion chimeras determines their properties—a biophysical characterization
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SYSNO ASEP 0543260 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název The order of PDZ3 and TrpCage in fusion chimeras determines their properties—a biophysical characterization Tvůrce(i) Boušová, Kristýna (UOCHB-X) ORCID
Bednárová, Lucie (UOCHB-X) RID, ORCID
Zouharová, Monika (UOCHB-X) ORCID
Vetýšková, Veronika (UOCHB-X) ORCID
Poštulková, Klára (UOCHB-X) ORCID
Hofbauerová, Kateřina (MBU-M) ORCID
Petrvalská, Olivia (FGU-C) RID, ORCID, SAI
Vaněk, O. (CZ)
Tripsianes, K. (CZ)
Vondrášek, Jiří (UOCHB-X) RID, ORCIDZdroj.dok. Protein Science. - : Wiley - ISSN 0961-8368
Roč. 30, č. 8 (2021), s. 1653-1666Poč.str. 14 s. Jazyk dok. eng - angličtina Země vyd. US - Spojené státy americké Klíč. slova chimeras ; fusion protein ; protein domains ; protein dynamic studies Obor OECD Biochemistry and molecular biology CEP EF16_019/0000729 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy GA19-03488S GA ČR - Grantová agentura ČR Způsob publikování Omezený přístup Institucionální podpora UOCHB-X - RVO:61388963 ; MBU-M - RVO:61388971 ; FGU-C - RVO:67985823 UT WOS 000657449100001 EID SCOPUS 85107179666 DOI 10.1002/pro.4107 Anotace Most of the structural proteins known today are composed of domains that carry their own functions while keeping their structural properties. It is supposed that such domains, when taken out of the context of the whole protein, can retain their original structure and function to a certain extent. Information on the specific functional and structural characteristics of individual domains in a new context of artificial fusion proteins may help to reveal the rules of internal and external domain communication. Moreover, this could also help explain the mechanism of such communication and address how the mutual allosteric effect plays a role in a such multi-domain protein system. The simple model system of the two-domain fusion protein investigated in this work consisted of a well-folded PDZ3 domain and an artificially designed small protein domain called Tryptophan Cage (TrpCage). Two fusion proteins with swapped domain order were designed to study their structural and functional features as well as their biophysical properties. The proteins composed of PDZ3 and TrpCage, both identical in amino acid sequence but different in composition (PDZ3-TrpCage, TrpCage-PDZ3), were studied using circualr dichroism (CD) spectrometry, analytical ultracentrifugation, and molecular dynamic simulations. The biophysical analysis uncovered different structural and denaturation properties of both studied proteins, revealing their different unfolding pathways and dynamics. Pracoviště Ústav organické chemie a biochemie Kontakt asep@uochb.cas.cz ; Kateřina Šperková, Tel.: 232 002 584 ; Viktorie Chládková, Tel.: 232 002 434 Rok sběru 2022 Elektronická adresa https://doi.org/10.1002/pro.4107
Počet záznamů: 1