Abstract
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.
Highlights
The process of amyloid transformation is associated with the reproduction of structural forms of β-structure type [1]
The analysis focuses on the role of edge fragments—β-sheet components due to the possibility of interaction resulting in the formation of amyloid-like complexes
This paper shows the role of edge β-strands in β-sheets relying in introduction a disorder of the ordering form present in β-sheets
Summary
The process of amyloid transformation is associated with the reproduction of structural forms of β-structure type [1]. The helical structure does not create conditions for propagation. The native protein structure guarantees stability and prevents the formation of complexes in an uncontrolled manner [2]. In the proteins’ activity, there is a need for complexation, necessary for their activity, whose control protects against uncontrolled aggregation [3]. Amyloid transformation can be caused by the presence of mutations, but it occurs with respect to the native form of proteins [4]. The activity of proteins is accompanied by the possibility of dynamic structure change
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