Examination of the conformational dynamics of photoregulated Concanavalin a by time-resolved light scattering

Eran Zahavy; Shai Rubin; Itamar Willner

doi:10.1039/C39930001753

Examination of the conformational dynamics of photoregulated Concanavalin a by time-resolved light scattering

Eran Zahavy
, Shai Rubin
, Itamar Willner^*

^*Corresponding author for this work

Institute of Chemistry

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

19 Scopus citations

Abstract

Spiropyran-modified Concanavalin A (Con-A) displays photoregulated binding towards α-D-mannopyranoside, the photostimulated binding of the substrate originating from a structural perturbation of the protein upon photoisomerization of spiro-Con-A to the zwitterionic Con-A; time-resolved light scattering reveals that the structural change of the protein involves a shrinkage, and the dynamics of the protein shrinkage depend on the loading of Con-A with spiropyran units.

Original language	English
Pages (from-to)	1753-1755
Number of pages	3
Journal	Chemical Communications
Issue number	23
DOIs	https://doi.org/10.1039/C39930001753
State	Published - 1993

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abstract = "Spiropyran-modified Concanavalin A (Con-A) displays photoregulated binding towards α-D-mannopyranoside, the photostimulated binding of the substrate originating from a structural perturbation of the protein upon photoisomerization of spiro-Con-A to the zwitterionic Con-A; time-resolved light scattering reveals that the structural change of the protein involves a shrinkage, and the dynamics of the protein shrinkage depend on the loading of Con-A with spiropyran units.",

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AU - Willner, Itamar

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N2 - Spiropyran-modified Concanavalin A (Con-A) displays photoregulated binding towards α-D-mannopyranoside, the photostimulated binding of the substrate originating from a structural perturbation of the protein upon photoisomerization of spiro-Con-A to the zwitterionic Con-A; time-resolved light scattering reveals that the structural change of the protein involves a shrinkage, and the dynamics of the protein shrinkage depend on the loading of Con-A with spiropyran units.

AB - Spiropyran-modified Concanavalin A (Con-A) displays photoregulated binding towards α-D-mannopyranoside, the photostimulated binding of the substrate originating from a structural perturbation of the protein upon photoisomerization of spiro-Con-A to the zwitterionic Con-A; time-resolved light scattering reveals that the structural change of the protein involves a shrinkage, and the dynamics of the protein shrinkage depend on the loading of Con-A with spiropyran units.

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Examination of the conformational dynamics of photoregulated Concanavalin a by time-resolved light scattering

Abstract

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