The relationship between relative solvent accessible surface area (rASA) and irregular structures in protean segments (ProSs)
| العنوان: | The relationship between relative solvent accessible surface area (rASA) and irregular structures in protean segments (ProSs) |
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| المؤلفون: | Divya Shaji |
| المصدر: | Bioinformation |
| بيانات النشر: | Biomedical Informatics, 2016. |
| سنة النشر: | 2016 |
| مصطلحات موضوعية: | protean segments (ProSs), 0301 basic medicine, Protein interface, Intrinsically disordered proteins, Chemistry, protein-protein interactions, General Medicine, Hypothesis, Accessible surface area, Protein–protein interaction, relative solvent accessible surface area (rASA), 03 medical and health sciences, Crystallography, 030104 developmental biology, secondary structure elements (SSEs), protein interface, Protein secondary structure, Alpha helix |
| الوصف: | 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. |
| تدمد: | 0973-2063 0973-8894 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::614c931d56b035741535d27433867b4aTest https://doi.org/10.6026/97320630012381Test |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....614c931d56b035741535d27433867b4a |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 09732063 09738894 |
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