Answers are grounded in this paper and cite their sources.
Nuclear magnetic resonance study demonstrates slow conformational switching in human beta-2 adrenergic receptors, indicating substantial structural rearrangements during agonist activation.
Proteins in slow motion: 19F NMR studies indicate that equilibria between active and inactive states of the human β2-adrenergic receptor require extensive structural rearrangements (arrows in picture). This was shown by an enthalpy difference of ΔHo≈40 kJ mol−1 and a slow exchange rate, with kex≪10 s−1.
No takes yet. Share an insight, caveat, or question.
Horst et al. (2013) studied this question.
Synapse has enriched 10 related papers. Consider them for comparative context: