Random protein sequences can form defined secondary structures and are well-tolerated in vivo

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F17%3A00482917" target="_blank" >RIV/61388963:_____/17:00482917 - isvavai.cz</a>

Alternative codes found

RIV/00216208:11310/17:10366951 RIV/00216208:11320/17:10366951

Result on the web

<a href="https://www.nature.com/articles/s41598-017-15635-8" target="_blank" >https://www.nature.com/articles/s41598-017-15635-8</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1038/s41598-017-15635-8" target="_blank" >10.1038/s41598-017-15635-8</a>

Result language

angličtina

Original language name

Random protein sequences can form defined secondary structures and are well-tolerated in vivo

Original language description

The protein sequences found in nature represent a tiny fraction of the potential sequences that could be constructed from the 20-amino-acid alphabet. To help define the properties that shaped proteins to stand out from the space of possible alternatives, we conducted a systematic computational and experimental exploration of random (unevolved) sequences in comparison with biological proteins. In our study, combinations of secondary structure, disorder, and aggregation predictions are accompanied by experimental characterization of selected proteins. We found that the overall secondary structure and physicochemical properties of random and biological sequences are very similar. Moreover, random sequences can be well-tolerated by living cells. Contrary to early hypotheses about the toxicity of random and disordered proteins, we found that random sequences with high disorder have low aggregation propensity( unlike random sequences with high structural content) and were particularly well-tolerated. This direct structure content/aggregation propensity dependence differentiates random and biological proteins. Our study indicates that while random sequences can be both structured and disordered, the properties of the latter make them better suited as progenitors (in both in vivo and in vitro settings) for further evolution of complex, soluble, three-dimensional scaffolds that can perform specific biochemical tasks.

Czech name

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Czech description

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Type

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

CEP classification

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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

2017

Confidentiality

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

Name of the periodical

Scientific Reports

ISSN

2045-2322

e-ISSN

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Volume of the periodical

7

Issue of the periodical within the volume

Nov 13

Country of publishing house

GB - UNITED KINGDOM

Number of pages

9

Pages from-to

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UT code for WoS article

000415023200010

EID of the result in the Scopus database

2-s2.0-85034090697