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Thiazole–amino acids: influence of thiazole ring on conformational properties of amino acid residues

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F21%3A00542031" target="_blank" >RIV/61388963:_____/21:00542031 - isvavai.cz</a>

  • Result on the web

    <a href="https://doi.org/10.1007/s00726-021-02974-0" target="_blank" >https://doi.org/10.1007/s00726-021-02974-0</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1007/s00726-021-02974-0" target="_blank" >10.1007/s00726-021-02974-0</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Thiazole–amino acids: influence of thiazole ring on conformational properties of amino acid residues

  • Original language description

    Post-translational modified thiazole–amino acid (Xaa–Tzl) residues have been found in macrocyclic peptides (e.g., thiopeptides and cyanobactins), which mostly inhibit protein synthesis in Gram + bacteria. Conformational study of the series of model compounds containing this structural motif with alanine, dehydroalanine, dehydrobutyrine and dehydrophenylalanine were performed using DFT method in various environments. The solid-state crystal structure conformations of thiazole–amino acid residues retrieved from the Cambridge Structural Database were also analysed. The studied structural units tend to adopt the unique semi-extended β2 conformation, which is stabilised mainly by N–H⋯NTzl hydrogen bond, and for dehydroamino acids also by π-electron conjugation. The conformational preferences of amino acids with a thiazole ring were compared with oxazole analogues and the role of the sulfur atom in stabilising the conformations of studied peptides was discussed.

  • 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

    10403 - Physical chemistry

Result continuities

  • Project

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2021

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Amino Acids

  • ISSN

    0939-4451

  • e-ISSN

    1438-2199

  • Volume of the periodical

    53

  • Issue of the periodical within the volume

    5

  • Country of publishing house

    AT - AUSTRIA

  • Number of pages

    14

  • Pages from-to

    673-686

  • UT code for WoS article

    000638833600001

  • EID of the result in the Scopus database

    2-s2.0-85104241621