The relationship between relative solvent accessible surface area (rASA) and irregular structures in protean segments (ProSs).

Divya Shaji

doi:10.6026/97320630012381

Abstract

Intrinsically Disordered Proteins (IDPs) lack a stable, three-dimensional structure under physiological conditions, yet they exhibit numerous biological activities. Protean segments (ProSs) are the functional regions of intrinsically disordered proteins that undergo disorder-to-order transitions upon binding to their partners. Example ProSs collected from the intrinsically disordered proteins with extensive annotations and literature (IDEAL) database. The interface of protean segments (ProSs) is classified into core, rim, and support, and analyzed their secondary structure elements (SSEs) based on the relative accessible surface area (rASA). The amino acid compositions and the relative solvent accessible surface areas (rASAs) of ProS secondary structural elements (SSEs) at the interface, core and rim were compared to those of heterodimers. The average number of contacts of alpha helices and irregular residues was calculated for each ProS and heterodimer. Furthermore, the ProSs were classified into high and low efficient based on their average number of contacts at the interface. The results indicate that the irregular structures of ProSs and heterodimers are significantly different. The rASA of irregular structures in the monomeric state (rASAm) is large, leads to the formation of larger ΔrASA and many contacts in ProSs.

Highlights

An intrinsically disordered protein (IDP) is a protein that is disordered in the unbound state and undergoes a disorder-to-order transition upon binding to their partners [1,2,3]
The key to effective interactions of Protean segments (ProSs) is the solvent exposure of rim residues in the monomeric state [13]
The content of irregular structures and beta strands are the largest difference between ProSs and heterodimers

Summary

Introduction

An intrinsically disordered protein (IDP) is a protein that is disordered (as a whole or in part) in the unbound state and undergoes a disorder-to-order transition upon binding to their partners [1,2,3] These IDPs have numerous biological activities such as signal transduction and transcriptional regulation and are highly abundant in nature [2, 4]. These proteins are associated with various human diseases, including cancer, cardiovascular disease, neurodegenerative diseases and amyloidoses [5,6,7]. The average number of contacts of ProS interface with its interaction partners is greater than that of heterodimers This indicates the effective interactions of ProSs that take place in the rim region like core. The key to effective interactions of ProSs is the solvent exposure of rim residues in the monomeric state (rASAm) [13]

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Conclusion