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@article{1784538, author = {Bousova, K. and Bednarova, L. and Zouharova, M. and Vetyskova, V. and Postulkova, K. and Hofbauerova, K. and Petrvalska, O. and Vanek, O. and Tripsianes, Konstantinos and Vondrasek, J.}, article_location = {HOBOKEN}, article_number = {8}, doi = {http://dx.doi.org/10.1002/pro.4107}, keywords = {chimeras; fusion protein; protein domains; protein dynamic studies}, language = {eng}, issn = {0961-8368}, journal = {Protein Science}, title = {The order of PDZ3 and TrpCage in fusion chimeras determines their properties-a biophysical characterization}, url = {https://www.ncbi.nlm.nih.gov/pubmed/33969912}, volume = {30}, year = {2021} }
TY - JOUR ID - 1784538 AU - Bousova, K. - Bednarova, L. - Zouharova, M. - Vetyskova, V. - Postulkova, K. - Hofbauerova, K. - Petrvalska, O. - Vanek, O. - Tripsianes, Konstantinos - Vondrasek, J. PY - 2021 TI - The order of PDZ3 and TrpCage in fusion chimeras determines their properties-a biophysical characterization JF - Protein Science VL - 30 IS - 8 SP - 1653-1666 EP - 1653-1666 PB - JOHN WILEY & SONS INC SN - 09618368 KW - chimeras KW - fusion protein KW - protein domains KW - protein dynamic studies UR - https://www.ncbi.nlm.nih.gov/pubmed/33969912 N2 - 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. ER -
BOUSOVA, K., L. BEDNAROVA, M. ZOUHAROVA, V. VETYSKOVA, K. POSTULKOVA, K. HOFBAUEROVA, O. PETRVALSKA, O. VANEK, Konstantinos TRIPSIANES and J. VONDRASEK. The order of PDZ3 and TrpCage in fusion chimeras determines their properties-a biophysical characterization. \textit{Protein Science}. HOBOKEN: JOHN WILEY \&{}amp; SONS INC, 2021, vol.~30, No~8, p.~1653-1666. ISSN~0961-8368. Available from: https://dx.doi.org/10.1002/pro.4107.
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