Thioester

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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. ❋ Unknown (2006)

Two of the thioester proteins, SpC3 and SpC3-2, are known to be expressed, respectively, in coelomocytes and in embryos and larvae. ❋ Unknown (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. ❋ Unknown (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. ❋ Unknown (2009)

These peptides interact with the same nucleobases found in DNA, but each nucleobase is bound to an organic compound known as a thioester. ❋ Unknown (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. ❋ Takashi Kawakami (2009)

Expression systems based on self-cleavable intein domains allow the generation of recombinant proteins with a C-terminal thioester. ❋ Unknown (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. ❋ Unknown (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. ❋ Unknown (2008)

Introduction of a MESNA / diMESNA redox couple resulted in simultaneous on-column refolding, purification and thioester generation of the model protein Ribonuclease A. ❋ Unknown (2008)

Unfortunately, common refolding procedures for recombinant proteins that contain disulfide bonds do not preserve the thioester functionality and therefore novel refolding procedures need to be developed. ❋ Unknown (2008)

The C-terminal thioester was shown to be active in native chemical ligation. ❋ Unknown (2008)

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