Title

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

Authors

Divya Shaji*

Affiliation

Graduate School of Information Science, Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-8601, Japan

Email

Divya Shaji – E-mail: dshaji@force.cs.is.nagoya-u.ac.jp; * Corresponding author

Article Type

Hypothesis

Date

Received October 19, 2016; Accepted November 18, 2016; Published November 28, 2016

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.

Keywords:

Intrinsically disordered proteins, secondary structure elements (SSEs), protein interface, relative solvent accessible surface area (rASA), protein-protein interactions, protean segments (ProSs).

Citation

D. Shaji, Bioinformation 12(9): 381-387 (2016)

Edited by

P Kangueane

ISSN

0973-2063

Publisher

Biomedical Informatics

License

This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.