Opsin shift in an aldolase antibody

Flavio Grynszpan; Ehud Keinan

doi:10.1016/S0960-894X(99)00406-0

Opsin shift in an aldolase antibody

Flavio Grynszpan
, Ehud Keinan

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

1 Scopus citations

Abstract

An antibody-retinal assembly that mimics the opsin shift (OS) of the naturally occurring visual pigments is reported. Both experiments and calculations show that the aldolase antibody 33F12 covalently binds all-trans retinal via a protonated Schiff base with a lysine residue. This chromophore, which exhibits a remarkable opsin red shift (140 nm), represents a useful model system for studying the factors that contribute to the OS.

Original language	English
Pages (from-to)	2419-2424
Number of pages	6
Journal	Bioorganic and Medicinal Chemistry Letters
Volume	9
Issue number	16
DOIs	https://doi.org/10.1016/S0960-894X(99)00406-0
State	Published - 16 Aug 1999
Externally published	Yes

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10.1016/S0960-894X(99)00406-0

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title = "Opsin shift in an aldolase antibody",

abstract = "An antibody-retinal assembly that mimics the opsin shift (OS) of the naturally occurring visual pigments is reported. Both experiments and calculations show that the aldolase antibody 33F12 covalently binds all-trans retinal via a protonated Schiff base with a lysine residue. This chromophore, which exhibits a remarkable opsin red shift (140 nm), represents a useful model system for studying the factors that contribute to the OS.",

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AB - An antibody-retinal assembly that mimics the opsin shift (OS) of the naturally occurring visual pigments is reported. Both experiments and calculations show that the aldolase antibody 33F12 covalently binds all-trans retinal via a protonated Schiff base with a lysine residue. This chromophore, which exhibits a remarkable opsin red shift (140 nm), represents a useful model system for studying the factors that contribute to the OS.

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Opsin shift in an aldolase antibody

Abstract

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