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      Thermodynamics of antagonist binding to rat muscarinic M2 receptors: antimuscarinics of the pridinol, sila-pridinol, diphenidol and sila-diphenidol type

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          Most cited references 36

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          Muscarinic receptor subtypes.

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            The Thermodynamic Basis of the Stability of Proteins, Nucleic Acids, and Membranes

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              Fundamental difference between the molecular interactions of agonists and antagonists with the beta-adrenergic receptor.

              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.
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                Author and article information

                Journal
                British Journal of Pharmacology
                Wiley
                00071188
                June 1993
                June 1993
                July 19 2012
                : 109
                : 2
                : 360-370
                Article
                10.1111/j.1476-5381.1993.tb13578.x
                © 2012

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