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

  • Mateusz Banach , Zdzisław Wiśniowski EMAIL logo , Magdalena Ptak and Irena Roterman
Published/Copyright: July 4, 2019
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Abstract

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.

Award Identifier / Grant number: K/ZDS/006363

Funding statement: The work was financially supported by the Jagiellonian University Medical College grant systems (Funder Id: http://dx.doi.org/10.13039/100009045, grant no. K/ZDS/006363).

  1. Ethical Approval: The conducted research is not related to either human or animal use.

  2. Author contributions: All the authors have accepted responsibility for the entire content of this submitted manuscript and approved submission.

  3. Employment or leadership: None declared.

  4. Honorarium: None declared.

  5. Competing interests: The funding organization(s) played no role in the study design; in the collection, analysis, and interpretation of data; in the writing of the report; or in the decision to submit the report for publication.

  6. Conflict of interests: The authors declare no conflict of interest.

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Received: 2019-05-15
Accepted: 2019-06-04
Published Online: 2019-07-04

© 2019 Walter de Gruyter GmbH, Berlin/Boston

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