Abstract
Antagonist binding to the beta-adrenergic receptor is largely entropy driven, with only a small enthalpy component. The binding of agonists, on the other hand, is associated with a large decrease in enthalpy which permits a highly unfavourable decrease in entropy. The thermodynamic differences between the binding of agonists and antagonists may provide new insights into the molecular basis for hormone stimulation of adenylate cyclase activity.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Adenylyl Cyclases / blood
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Adrenergic beta-Agonists / metabolism*
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Adrenergic beta-Antagonists / metabolism*
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Animals
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Enzyme Activation / drug effects
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Erythrocyte Membrane / metabolism
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Ligands
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Receptors, Adrenergic / metabolism*
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Receptors, Adrenergic, beta / metabolism*
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Temperature
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Thermodynamics
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Turkeys
Substances
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Adrenergic beta-Agonists
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Adrenergic beta-Antagonists
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Ligands
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Receptors, Adrenergic
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Receptors, Adrenergic, beta
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Adenylyl Cyclases