Next Article in Journal
Multiobjective Optimization of a Plate Heat Exchanger in a Waste Heat Recovery Organic Rankine Cycle System for Natural Gas Engines
Next Article in Special Issue
Entropy and Information within Intrinsically Disordered Protein Regions
Previous Article in Journal
Information Theory Applications in Signal Processing
Previous Article in Special Issue
Prediction of MoRFs in Protein Sequences with MLPs Based on Sequence Properties and Evolution Information
Open AccessCommunication

Sequence Versus Composition: What Prescribes IDP Biophysical Properties?

Institute of Organic Chemistry and Biochemitry of the Czech Academy of Sciences, Flemingovo náměstí 2, 166 10 Praha 6 Prague, Czech Republic
Department of Cell Biology, Faculty of Science, Charles University, Viničná 7, 128 43 Praha 2 Prague, Czech Republic
Authors to whom correspondence should be addressed.
Entropy 2019, 21(7), 654;
Received: 13 May 2019 / Revised: 26 June 2019 / Accepted: 28 June 2019 / Published: 3 July 2019
Intrinsically disordered proteins (IDPs) represent a distinct class of proteins and are distinguished from globular proteins by conformational plasticity, high evolvability and a broad functional repertoire. Some of their properties are reminiscent of early proteins, but their abundance in eukaryotes, functional properties and compositional bias suggest that IDPs appeared at later evolutionary stages. The spectrum of IDP properties and their determinants are still not well defined. This study compares rudimentary physicochemical properties of IDPs and globular proteins using bioinformatic analysis on the level of their native sequences and random sequence permutations, addressing the contributions of composition versus sequence as determinants of the properties. IDPs have, on average, lower predicted secondary structure contents and aggregation propensities and biased amino acid compositions. However, our study shows that IDPs exhibit a broad range of these properties. Induced fold IDPs exhibit very similar compositions and secondary structure/aggregation propensities to globular proteins, and can be distinguished from unfoldable IDPs based on analysis of these sequence properties. While amino acid composition seems to be a major determinant of aggregation and secondary structure propensities, sequence randomization does not result in dramatic changes to these properties, but for both IDPs and globular proteins seems to fine-tune the tradeoff between folding and aggregation. View Full-Text
Keywords: IDP; IDR; sequence randomization; secondary structure prediction; aggregation propensity IDP; IDR; sequence randomization; secondary structure prediction; aggregation propensity
Show Figures

Figure 1

MDPI and ACS Style

Vymětal, J.; Vondrášek, J.; Hlouchová, K. Sequence Versus Composition: What Prescribes IDP Biophysical Properties? Entropy 2019, 21, 654.

Show more citation formats Show less citations formats
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

Back to TopTop