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Open AccessArticle

The Status of Edge Strands in Ferredoxin-Like Fold

Department of Bioinformatics and Telemedicine, Jagiellonian University - Medical College, Lazarza 16, 31-533 Krakow, Poland
Institute of Computer Science, Silesian University of Technology, Akademicka 16, 44-100 Gliwice, Poland
Chair of Medical Biochemistry - Jagiellonian University - Medical College, Kopernika 7, 31-034 Krakow, Poland
Author to whom correspondence should be addressed.
Symmetry 2020, 12(6), 1032;
Received: 20 May 2020 / Revised: 17 June 2020 / Accepted: 17 June 2020 / Published: 19 June 2020
There is an opinion in professional literature that edge-strands in β-sheet are critical to the processes of amyloid transformation. Propagation of fibrillar forms mainly takes place on the basis of β-sheet type interactions. In many proteins, the edge strands represent only a partially matched form to the β-sheet. Therefore, the edge-strand takes slightly distorted forms. The assessment of the level of arrangement can be carried out based on studying the secondary structure as well as the structure of the hydrophobic core. For this purpose, a fuzzy oil drop model was used to determine the contribution of each fragment with a specific secondary structure to the construction of the system being the effect of a certain synergy, which results in the construction of a hydrophobic core. Studying the participation of β-sheets edge fragments in the hydrophobic core construction is the subject of the current analysis. Statuses of these edge fragments in β-sheets in ferredoxin-like folds are treated as factors that disturb the symmetry of the system. View Full-Text
Keywords: β-strand; β-sheet; edge β-strand; hydrophobicity; hydrophobic core; synergy; symmetry β-strand; β-sheet; edge β-strand; hydrophobicity; hydrophobic core; synergy; symmetry
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Banach, M.; Fabian, P.; Stapor, K.; Konieczny, L.; Ptak-Kaczor, M.; Roterman, I. The Status of Edge Strands in Ferredoxin-Like Fold. Symmetry 2020, 12, 1032.

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