An Academy of Sciences, 142290 Pushchino, Russia Institute of Mathematical Difficulties of Biology RAS–The Branch of Keldysh Institute of Applied Mathematics of Russian Academy of Sciences, 142290 Pushchino, Russia Correspondence: kristina.malsagova86@gmail; Tel.: 7-499-764-Abstract: Proteins expressed throughout the cell cycle figure out cell function, topology, and responses to environmental influences. The development and improvement of experimental approaches inside the field of structural biology supply useful data concerning the structure and functions of person proteins. This function is devoted for the study of supersecondary structures of proteins and determination of their structural motifs, description of experimental strategies for their detection, databases, and repositories for storage, at the same time as solutions of molecular dynamics analysis. The interest within the study of supersecondary structures in proteins is resulting from their autonomous stability outdoors the protein globule, which makes it doable to study folding processes, conformational alterations in protein isoforms, and aberrant proteins with higher productivity.Citation: Rudnev, V.R.; Kulikova, L.I.; Nikolsky, K.S.; Malsagova, K.A.; Kopylov, A.T.; Kaysheva, A.L. Present Approaches in Supersecondary Structures Investigation. Int. J. Mol. Sci. 2021, 22, 11879. 10.3390/ ijms222111879 Academic Editor: Antonio Rosato Received: 21 JNJ-42253432 In Vitro September 2021 Accepted: 29 October 2021 Published: 2 NovemberKeywords: structural motifs of proteins; helical pairs; experimental procedures; databases1. Introduction Very simple structural motifs consisting of a number of components of secondary structure with unique polypeptide chain folding are objects drawing focus. The interest is raised due to the uniqueness of those structures and their potential to become embryos in protein folding [1]. When modeling a protein structure or predicting its tertiary structure, motifs could be a starting point in browsing for doable folds of polypeptide chains, or used as steady structures in protein studies. Efimov et al. presented a classification of structural motifs consisting of -helices and -strands having unique folds [1]. Probably the most widespread structural motifs in homologous and non-homologous proteins are –corner, –corner, — and –hairpins, —motif and 3-corner [2]. The –corner is arranged by two -helices, that are connected by the polypeptide chain. This is a compact spatial structure with a hydrophobic core along with a polar shell. Side chains of residues fully buried in a hydrophobic core are hydrophobic [2]. The –hairpins and –corners is usually referred to as -strands containing supersecondary structures. The –corner is often believed as a long –hairpin folded upright towards itself, so strands Donepezil-d5 AChE rotate towards the correct about an imaginary axis as they move from one particular layer to a different. The –hairpin, which organizes the helical coil structure or –corner, is right-handed when viewed in the concave side [3]. The —motif is usually a mixed form of SSS (supersecondary structure) [3]. This motif is a lot more complicated in terms of structural organization in comparison with — and –hairpins, and consists of two parallel -strands connected by an -helix. Connection in between helixes can differ drastically in length plus the axis of helix is roughly parallel for the -strands; thereby all three components interact to form a hydrophobic core. Amongst all identified proteins, quite a few small proteins consist of only one particular or two identified structural motifs. This indicates that such structural motifs are a.