Sequence Versus Composition: What Prescribes IDP Biophysical Properties?

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F19%3A00508837" target="_blank" >RIV/61388963:_____/19:00508837 - isvavai.cz</a>

Alternative codes found

RIV/00216208:11310/19:10403744

Result on the web

<a href="https://www.mdpi.com/1099-4300/21/7/654" target="_blank" >https://www.mdpi.com/1099-4300/21/7/654</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.3390/e21070654" target="_blank" >10.3390/e21070654</a>

Result language

angličtina

Original language name

Sequence Versus Composition: What Prescribes IDP Biophysical Properties?

Original language description

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.

Czech name

—

Czech description

—

Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

—

OECD FORD branch

10608 - Biochemistry and molecular biology

Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year

2019

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Entropy

ISSN

1099-4300

e-ISSN

—

Volume of the periodical

21

Issue of the periodical within the volume

7

Country of publishing house

CH - SWITZERLAND

Number of pages

8

Pages from-to

654

UT code for WoS article

000478585200086

EID of the result in the Scopus database

2-s2.0-85068936317