Site-specific incorporation of photoisomerizable azobenzene groups into ribonuclease S

David Liu; John Karanicolas; Catherine Yu; Zhihua Zhang; G. Andrew Woolley

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

Site-specific incorporation of photoisomerizable azobenzene groups into ribonuclease S

David Liu, John Karanicolas, Catherine Yu, Zhihua Zhang, G. Andrew Woolley

Cancer Signaling and Microenvironment (CSM)

University of Toronto

Research output: Contribution to journal › Article › peer-review

57 Scopus citations

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.

Original language	English
Pages (from-to)	2677-2680
Number of pages	4
Journal	Bioorganic and Medicinal Chemistry Letters
Volume	7
Issue number	20
DOIs	https://doi.org/10.1016/S0960-894X(97)10044-0
State	Published - Oct 21 1997

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title = "Site-specific incorporation of photoisomerizable azobenzene groups into ribonuclease S",

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.",

author = "David Liu and John Karanicolas and Catherine Yu and Zhihua Zhang and Woolley, {G. Andrew}",

year = "1997",

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T1 - Site-specific incorporation of photoisomerizable azobenzene groups into ribonuclease S

AU - Liu, David

AU - Karanicolas, John

AU - Yu, Catherine

AU - Zhang, Zhihua

AU - Woolley, G. Andrew

PY - 1997/10/21

Y1 - 1997/10/21

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0030668155&partnerID=8YFLogxK

U2 - 10.1016/S0960-894X(97)10044-0

DO - 10.1016/S0960-894X(97)10044-0

M3 - Article

AN - SCOPUS:0030668155

SN - 0960-894X

VL - 7

SP - 2677

EP - 2680

JO - Bioorganic and Medicinal Chemistry Letters

JF - Bioorganic and Medicinal Chemistry Letters

IS - 20

ER -

Site-specific incorporation of photoisomerizable azobenzene groups into ribonuclease S

Abstract

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