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Allosteric Effects: Binding Cooperativity in a Subunit Model
Author(s) -
Rebek J.,
Wattley R. V.,
Costello T.,
Gadwood R.,
Marshall L.
Publication year - 1981
Publication title -
angewandte chemie international edition in english
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 0570-0833
DOI - 10.1002/anie.198106051
Subject(s) - cooperativity , allosteric regulation , cooperative binding , protein subunit , chemistry , binding site , allosteric enzyme , biophysics , stereochemistry , enzyme , biochemistry , biology , gene
The macrobicyclic polyether (1) is the first “small” model system which exhibits a binding cooperativity. It could be shown by 600‐MHz 1 H‐NMR studies that binding of one Hg(CN) 2 to (1) increases its binding ability for a second Hg(CN) 2 by a factor of ten.
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