This transdermal delivery system allows the mitochondria to receive increased levels of this protective tripeptide. ❋ M.D. Nicholas Perricone (2010)
Glutathione is a tripeptide, a molecule composed of three amino acids, and is the most abundant and important antioxidant protective system in our cells. ❋ M.D. Nicholas Perricone (2010)
The fluorescent moiety is an imidazolone ring structure that is formed by the posttranslational cyclization of a tripeptide, ser65-tyr66-gly67. ❋ William Harryman (2009)
Syn-Ake, as the compound is called, is made from a synthetic tripeptide that copies the effect of a peptide found in the venom of the Temple Viper, found in the Snake Temple of Penang, Malaysia. ❋ Unknown (2009)
Denaturation of green fluorescent protein destroys fluorescence, as might be expected, and mutations to residues surrounding the tripeptide fluorophore can dramatically alter the fluorescence properties. ❋ Unknown (2005)
The second important feature of green fluorescent protein is that fluorescence is highly dependent on the molecular structure surrounding the tripeptide fluorophore. ❋ Unknown (2005)
If one of these protecting groups in the dipeptide is later selectively removed and reaction with a third amino acid containing one protected group carried out, a tripeptide is formed. ❋ Unknown (1984)
Synthesis of a tripeptide using Merrifield´s methology. ❋ Unknown (1984)
Synthesis of a tripeptide using conventional methodology. ❋ Unknown (1984)
This dipeptide is then combined with a third modified amino acid to give a tripeptide and so on. ❋ Unknown (1984)
During the years at Chicago Bloch also investigated (with J. Snoke) the enzymatic synthesis of the tripeptide glutathione. ❋ Unknown (1972)
Later he proved it to be the tripeptide of glutamic acid, glycine and cystein. ❋ Unknown (1965)
OppAMTB was capable of binding the tripeptide glutathione and the nonapeptide bradykinin, indicative of a somewhat broad substrate specificity. ❋ Arunava Dasgupta Et Al. (2010)
GSH/mg protein, suggesting that the tripeptide is preferred over the bulkier nonapeptide bradykinin. ❋ Arunava Dasgupta Et Al. (2010)
We observe that OppA is capable of binding both the tripeptide glutathione and the nonapeptide bradykinin. ❋ Arunava Dasgupta Et Al. (2010)
We present evidence that OppA binds to a wide range of peptides in terms of their size, ranging from the nonapeptide bradykinin to the tripeptide ❋ Arunava Dasgupta Et Al. (2010)
Thus, the presence of either of these tripeptide sequences in a polypeptide creates a potential glycosylation site. ❋ Unknown (2010)
The tripeptide sequences asparagine-X-serine and asparagine-X-threonine, where X is any amino acid except proline, are the recognition sequences for enzymatic attachment of the carbohydrate moiety to the asparagine side chain. ❋ Unknown (2010)
Addition of glycosylation sites to the antibody is conveniently accomplished by altering the amino acid sequence such that it contains one or more of the above-described tripeptide sequences (for N-linked glycosylation sites). ❋ Unknown (2010)
