Next Article in Journal
On the Absolute Stable Difference Scheme for Third Order Delay Partial Differential Equations
Previous Article in Journal
Existence Results of Mild Solutions for the Fractional Stochastic Evolution Equations of Sobolev Type
Open AccessArticle

The Status of Edge Strands in Ferredoxin-Like Fold

1
Department of Bioinformatics and Telemedicine, Jagiellonian University - Medical College, Lazarza 16, 31-533 Krakow, Poland
2
Institute of Computer Science, Silesian University of Technology, Akademicka 16, 44-100 Gliwice, Poland
3
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; https://doi.org/10.3390/sym12061032
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
Show Figures

Figure 1

MDPI and ACS Style

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.

Show more citation formats Show less citations formats
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Search more from Scilit
 
Search
Back to TopTop