The Hydrophobic Effect Has the Greatest Influence on Protein Stability. The hydrophobic effect, which causes nonpolar substances to minimize their contacts with water, is the major determinant of native protein structure.

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Three principal classes of G PCR that bind their ligand in different ways:

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Member of family A of GPCRs -β-adrenergic receptors

Member of family B of GPCRs -glucagon receptor 

Member of family C of GPCRs -glutamate receptor

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Binding of cAMP by an R subunit of PKA occurs in a cooperative fashion; i.e., binding of the first cAMP molecule to CNB-B lowers the Kd for binding of the second cAMP to CNB-A.

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The activated β2-adrenergic receptor induces GDP-->GTP exchange on a stimulatory G protein (Gs).