Aggregation-promoting conditions necessary to create the complexes by acylphosphatase from the hyperthermophile Sulfolobus solfataricus

• Autorzy: Banach Mateusz , Wiśniowski Zdzisław , Ptak Magdalena , Roterman Irena

Identyfikatory

DOI

10.1515/bams-2019-0023

• Języki publikacji: EN

Abstrakty

EN

The structural transition from the globular to the amyloid form of proteins requires aggregation-promoting conditions. The protein example of this category is acylphosphatase from the hyperthermophile Sulfolobus solfataricus. This protein represents a structure with a well-defined hydrophobic core. This is why the complexation (including oligomerization) of this protein is of low probability. The chain fragment participating in aggregation in comparison to the status with respect to the fuzzy oil drop model is discussed in this paper.

Słowa kluczowe

EN

aggregation-promoting conditions; amyloidosis; hydrophobicity

• Wydawca: Uniwersytet Jagielloński - Collegium Medicum ; De Gruyter
• Czasopismo: Bio-Algorithms and Med-Systems
• Rocznik: 2019
• Tom: Vol. 15, no. 2
• Strony: art. no. 20190023
• Opis fizyczny: Bibliogr. 30 poz., rys., tab.

Twórcy

autor

Banach Mateusz

• Department of Bioinformatics and Telemedicine, Jagiellonian University Medical College, Krakow, Poland

autor

Wiśniowski Zdzisław

• Department of Bioinformatics and Telemedicine, Jagiellonian University Medical College, Lazarza 16, 31-530 Krakow, Poland

autor

Ptak Magdalena

• Department of Bioinformatics and Telemedicine, Jagiellonian University Medical College, Krakow, Poland

autor

Roterman Irena

• Department of Bioinformatics and Telemedicine, Jagiellonian University Medical College, Krakow, Poland

Bibliografia

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Uwagi

Opracowanie rekordu ze środków MNiSW, umowa Nr 461252 w ramach programu "Społeczna odpowiedzialność nauki" - moduł: Popularyzacja nauki i promocja sportu (2020).