Definitions

from Wiktionary, Creative Commons Attribution/Share-Alike License.

  • noun organic chemistry Any of several classes of organic compound in which one or both oxygen atoms of an ester group are replaced by those of sulfur

Etymologies

Sorry, no etymologies found.

Support

Help support Wordnik (and make this page ad-free) by adopting the word thioester.

Examples

  • Two of the thioester proteins, SpC3 and SpC3-2, are known to be expressed, respectively, in coelomocytes and in embryos and larvae.

    The sea urchin genome - The Panda's Thumb 2006

  • The alternative pathway is initiated by members of the thioester protein family, which, in the sea urchin, was somewhat expanded with four genes.

    The sea urchin genome - The Panda's Thumb 2006

  • It is known that an adenylated substrate, bound to an E1 enzyme's adenylation site, forms a thioester link with a key cysteine at its other site, the Cys domain.

    Engineering News: Latest News 2010

  • It is known that an adenylated substrate, bound to an E1 enzyme's adenylation site, forms a thioester link with a key cysteine at its other site, the Cys domain.

    Engineering News: Latest News 2010

  • In this technique, one peptide fragment is attached to the terminal cysteine group (sulfur-containing amino acid) of a second peptide fragment by means of a thioester group-a selective reaction that results in a natural peptide bond.

    innovations-report 2009

  • These peptides interact with the same nucleobases found in DNA, but each nucleobase is bound to an organic compound known as a thioester.

    PhysOrg.com - latest science and technology news stories 2009

  • Expression of linear peptides bearing a cysteine-proline dipeptide sequence followed by glycolic acid results in self-rearrangement to a C-terminal diketopiperadine-thioester, which non-enzymatically generates a cyclized peptide.

    Naturejobs - All Jobs Takashi Kawakami 2009

  • Expression systems based on self-cleavable intein domains allow the generation of recombinant proteins with a C-terminal thioester.

    BioMed Central - Latest articles 2008

  • A novel redox buffer consisting of MESNA and diMESNA showed a refolding efficiency comparable to that of GSH / GSSG and prevented loss of the protein's thioester functionality.

    BioMed Central - Latest articles 2008

  • Moreover, introduction of the MESNA / diMESNA redox couple in the cleavage buffer allowed simultaneous on-column refolding of Ribonuclease A and intein-mediated cleavage to yield Ribonuclease A with a C-terminal MESNA-thioester.

    BioMed Central - Latest articles 2008

Comments

Log in or sign up to get involved in the conversation. It's quick and easy.