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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
Author(s) -
Payre Nathalie,
Cottaz Sylvain,
Boisset Claire,
Borsali Redouane,
Svensson Birte,
Henrissat Bernard,
Driguez Hugues
Publication year - 1999
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/(sici)1521-3773(19990401)38:7<974::aid-anie974>3.0.co;2-k
Subject(s) - dynamic light scattering , substrate (aquarium) , chemistry , cyclodextrin , schematic , starch , ligand (biochemistry) , diagram , light scattering , crystallography , acarbose , stereochemistry , scattering , materials science , biochemistry , enzyme , nanotechnology , optics , biology , physics , computer science , receptor , ecology , nanoparticle , database , electronic engineering , engineering
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).