Sequence Versus Composition: What Prescribes IDP Biophysical Properties?
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Institute of Organic Chemistry and Biochemitry of the Czech Academy of Sciences, Flemingovo náměstí 2, 166 10 Praha 6 Prague, Czech Republic
2
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; https://doi.org/10.3390/e21070654
Received: 13 May 2019
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Revised: 26 June 2019
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Accepted: 28 June 2019
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Published: 3 July 2019
(This article belongs to the Special Issue Information in Intrinsically Disordered Proteins and Complex Protein Networks)
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.
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MDPI and ACS Style
Vymětal, J.; Vondrášek, J.; Hlouchová, K. Sequence Versus Composition: What Prescribes IDP Biophysical Properties? Entropy 2019, 21, 654. https://doi.org/10.3390/e21070654
AMA Style
Vymětal J, Vondrášek J, Hlouchová K. Sequence Versus Composition: What Prescribes IDP Biophysical Properties? Entropy. 2019; 21(7):654. https://doi.org/10.3390/e21070654
Chicago/Turabian StyleVymětal, Jiří, Jiří Vondrášek, and Klára Hlouchová. 2019. "Sequence Versus Composition: What Prescribes IDP Biophysical Properties?" Entropy 21, no. 7: 654. https://doi.org/10.3390/e21070654
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