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Modern and prebiotic amino acids support distinct structural profiles in proteins

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F22%3A00559020" target="_blank" >RIV/61388963:_____/22:00559020 - isvavai.cz</a>

  • Alternative codes found

    RIV/00216208:11310/22:10450824

  • Result on the web

    <a href="https://doi.org/10.1098/rsob.220040" target="_blank" >https://doi.org/10.1098/rsob.220040</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1098/rsob.220040" target="_blank" >10.1098/rsob.220040</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Modern and prebiotic amino acids support distinct structural profiles in proteins

  • Original language description

    The earliest proteins had to rely on amino acids available on early Earth before the biosynthetic pathways for more complex amino acids evolved. In extant proteins, a significant fraction of the 'late' amino acids (such as Arg, Lys, His, Cys, Trp and Tyr) belong to essential catalytic and structure-stabilizing residues. How (or if) early proteins could sustain an early biosphere has been a major puzzle. Here, we analysed two combinatorial protein libraries representing proxies of the available sequence space at two different evolutionary stages. The first is composed of the entire alphabet of 20 amino acids while the second one consists of only 10 residues (ASDGLIPTEV) representing a consensus view of plausibly available amino acids through prebiotic chemistry. We show that compact conformations resistant to proteolysis are surprisingly similarly abundant in both libraries. In addition, the early alphabet proteins are inherently more soluble and refoldable, independent of the general Hsp70 chaperone activity. By contrast, chaperones significantly increase the otherwise poor solubility of the modern alphabet proteins suggesting their coevolution with the amino acid repertoire. Our work indicates that while both early and modern amino acids are predisposed to supporting protein structure, they do so with different biophysical properties and via different mechanisms.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10608 - Biochemistry and molecular biology

Result continuities

  • Project

    <a href="/en/project/GJ17-10438Y" target="_blank" >GJ17-10438Y: Terrestrial protein sequence and structure space evolution</a><br>

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2022

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Open Biology

  • ISSN

    2046-2441

  • e-ISSN

    2046-2441

  • Volume of the periodical

    12

  • Issue of the periodical within the volume

    6

  • Country of publishing house

    GB - UNITED KINGDOM

  • Number of pages

    11

  • Pages from-to

    220040

  • UT code for WoS article

    000814138000003

  • EID of the result in the Scopus database

    2-s2.0-85132280123