allosteric transition

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allosteric transition

[¦a·lə¦stir·ik tranz′ish·ən]
(biochemistry)
A reversible exchange of one base pair for another on a protein molecule that alters the properties of the active site and changes the biological activity of the protein.
McGraw-Hill Dictionary of Scientific & Technical Terms, 6E, Copyright © 2003 by The McGraw-Hill Companies, Inc.
References in periodicals archive ?
The classical or canonical model of signaling by cytokines such as the interferons (IFNs) involves ligand interaction with receptor extracellular domain, followed by "allosteric changes" in the receptor cytoplasmic domain that results in autophosphorylation of the relevant Janus tyrosine kinases (JAKs) and subsequent tyrosine phosphorylation of receptor cytoplasmic domain(s) [1-4].
Noncanonical IFN Signaling: Mechanistic Linkage of Genetic and Epigenetic Events
Bahar, "Allosteric changes in protein structure computed by a simple mechanical model: hemoglobin T [left and right arrow] R2 transition," Journal of Molecular Biology, vol.
Comparative Study of Elastic Network Model and Protein Contact Network for Protein Complexes: The Hemoglobin Case
These polyether brevetoxins and a number of synthetic derivatives have had some limited success in dissecting the various molecular allosteric changes thought to occur sequentially during ion channel topographic progression from closed to open to inactivated and back to the closed state.
Oceans and human health: a new era of environmental opportunities
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