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The order of PDZ3 and TrpCage in fusion chimeras determines their properties—a biophysical characterization

SYSNO ASEP	0543260
Document Type	J - Journal Article
R&D Document Type	Journal Article
Subsidiary J	Článek ve WOS
Title	The order of PDZ3 and TrpCage in fusion chimeras determines their properties—a biophysical characterization
Author(s)	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, ORCID}
Source Title	Protein Science. - : Wiley - ISSN 0961-8368 Roč. 30, č. 8 (2021), s. 1653-1666
Number of pages	14 s.
Language	eng - English
Country	US - United States
Keywords	chimeras ; fusion protein ; protein domains ; protein dynamic studies
OECD category	Biochemistry and molecular biology
R&D Projects	EF16_019/0000729 GA MŠMT - Ministry of Education, Youth and Sports (MEYS)
	GA19-03488S GA ČR - Czech Science Foundation (CSF)
Method of publishing	Limited access
Institutional support	UOCHB-X - RVO:61388963 ; MBU-M - RVO:61388971 ; FGU-C - RVO:67985823
UT WOS	000657449100001
EID SCOPUS	85107179666
DOI	10.1002/pro.4107
Annotation	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.
Workplace	Institute of Organic Chemistry and Biochemistry
Contact	asep@uochb.cas.cz ; Kateřina Šperková, Tel.: 232 002 584 ; Viktorie Chládková, Tel.: 232 002 434
Year of Publishing	2022
Electronic address	https://doi.org/10.1002/pro.4107

Number of the records: 1