Next Article in Journal
Terpenoids from the Octocoral Sinularia gaweli
Next Article in Special Issue
In Silico Analysis of Correlations between Protein Disorder and Post-Translational Modifications in Algae
Previous Article in Journal
Plasma-Derived Fibronectin Stimulates Chondrogenic Differentiation of Human Subchondral Cortico-Spongious Progenitor Cells in Late-Stage Osteoarthritis
Previous Article in Special Issue
Disorder Prediction Methods, Their Applicability to Different Protein Targets and Their Usefulness for Guiding Experimental Studies
Article Menu
Issue 8 (August) cover image

Export Article

Open AccessArticle
Int. J. Mol. Sci. 2015, 16(8), 19490-19507;

How Common Is Disorder? Occurrence of Disordered Residues in Four Domains of Life

Institute of Protein Research, Russian Academy of Sciences, Pushchino 142290, Moscow Region, Russia
Author to whom correspondence should be addressed.
Academic Editors: Lukasz Kurgan and Vladimir N. Uversky
Received: 2 July 2015 / Revised: 2 August 2015 / Accepted: 3 August 2015 / Published: 18 August 2015
Full-Text   |   PDF [1549 KB, uploaded 24 August 2015]   |  


Disordered regions play important roles in protein adaptation to challenging environmental conditions. Flexible and disordered residues have the highest propensities to alter the protein packing. Therefore, identification of disordered/flexible regions is important for structural and functional analysis of proteins. We used the IsUnstruct program to predict the ordered or disordered status of residues in 122 proteomes, including 97 eukaryotic and 25 large bacterial proteomes larger than 2,500,000 residues. We found that bacterial and eukaryotic proteomes contain comparable fraction of disordered residues, which was 0.31 in the bacterial and 0.38 in the eukaryotic proteomes. Additional analysis of the total of 1540 bacterial proteomes of various sizes yielded a smaller fraction of disordered residues, which was only 0.26. Together, the results showed that the larger is the size of the proteome, the larger is the fraction of the disordered residues. A continuous dependence of the fraction of disordered residues on the size of the proteome is observed for four domains of life: Eukaryota, Bacteria, Archaea, and Viruses. Furthermore, our analysis of 122 proteomes showed that the fraction of disordered residues increased with increasing the length of homo-repeats for polar, charged, and small residues, and decreased for hydrophobic residues. The maximal fraction of disordered residues was obtained for proteins containing lysine and arginine homo-repeats. The minimal fraction was found in valine and leucine homo-repeats. For 15-residue long homo-repeats these values were 0.2 (for Val and Leu) and 0.7 (for Lys and Arg). View Full-Text
Keywords: proteome; homo-repeats; disordered regions; computational prediction proteome; homo-repeats; disordered regions; computational prediction

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

Share & Cite This Article

MDPI and ACS Style

Lobanov, M.Y.; Galzitskaya, O.V. How Common Is Disorder? Occurrence of Disordered Residues in Four Domains of Life. Int. J. Mol. Sci. 2015, 16, 19490-19507.

Show more citation formats Show less citations formats

Related Articles

Article Metrics

Article Access Statistics



[Return to top]
Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top