Site-specific incorporation of photoisomerizable azobenzene groups into ribonuclease S

doi:10.1016/S0960-894X(97)10044-0

Bioorganic & Medicinal Chemistry Letters

Volume 7, Issue 20, 21 October 1997, Pages 2677-2680

https://doi.org/10.1016/S0960-894X(97)10044-0 Get rights and content

Abstract

Syntheses of S-peptide analogues bearing phenylazophenylalanine (Pap) residues at positions 4, 8, and 11 are described. Noncovalent reassociation of the Pap-4 and Pap-11 peptides with S-protein reconstitutes ribonuclease activity. Photoisomerization of the Pap-4 peptide is found to modulate the enzyme activity.

Noncovalent reassociation of S-peptide analogues bearing phenyl-azophenylalanine (Pap) residues with S-protein reconstitutes ribonuclease activity. Photoisomerization of the Pap-4 peptide modulates activity.

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Site-specific incorporation of photoisomerizable azobenzene groups into ribonuclease S

Abstract

Biochim Biophys Acta

J. Biol. Chem.

Anal. Biochem.

J. Biol. Chem.

Annu. Rev. Physiol.

J. Am. Chem. Soc.

J. Am. Chem. Soc.

J. Am. Chem. Soc.