Definitions
from Wiktionary, Creative Commons Attribution/Share-Alike License.
- noun organic chemistry Any of several classes of
organic compound in which one or bothoxygen atoms of anester group are replaced by those ofsulfur
Etymologies
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Examples
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Two of the thioester proteins, SpC3 and SpC3-2, are known to be expressed, respectively, in coelomocytes and in embryos and larvae.
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The alternative pathway is initiated by members of the thioester protein family, which, in the sea urchin, was somewhat expanded with four genes.
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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.
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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.
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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
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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
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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
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Expression systems based on self-cleavable intein domains allow the generation of recombinant proteins with a C-terminal thioester.
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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.
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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.
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