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Dynamic Light Scattering Evidence for a Ligand-Induced Motion between the Two Domains of Glucoamylase G1 of Aspergillus niger with Heterobivalent Substrate Analogues
Journal article   Peer reviewed

Dynamic Light Scattering Evidence for a Ligand-Induced Motion between the Two Domains of Glucoamylase G1 of Aspergillus niger with Heterobivalent Substrate Analogues

Nathalie Payre, Sylvain Cottaz, Claire Boisset, Redouane Borsali, Birte Svensson, Bernard Henrissat and Hugues Driguez
Angewandte Chemie (International ed.), Vol.38(7), pp.974-977
01/04/1999
DOI: https://doi.org/10.1002/(SICI)1521-3773(19990401)38:7<974::AID-ANIE974>3.0.CO;2-K
PMID: 29711862

Abstract

Carbohydrates Enzyme inhibitors Dynamic light scattering Structure-activity relationships Protein structures
Heterobifunctional ligands that bind at the same time to the catalytic domain and to the starch-binding domain of glucoamylase induce a conformational change of the protein, as shown by dynamic light scattering. The ligands consist of acarbose and β-cyclodextrin linked together by oligoethylene glycols of variable length (see the schematic diagram).

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