Figure 3.

Summaries of the graphs of the discrete wavelet transforms W^R of each Ψ^R (Left of each panel), the maximum entropy, complex poles power spectra h(ω) values of each peptide ligand (Upper Right of each panel), and the h(ω) of its receptor Ψ^R (Lower Right of each panel) for a representative set of peptide ligands and their G protein-coupled, transmembrane receptor sequences. The sequence lengths along the abscissa of the W^R plots (receptor length in amino acid residues minus the lag of the autocovariance matrix) are as follows: KAPPA OPIOID RECEPTOR (REC). = 362, MU OPIOID REC. = 402, ORPHAN OPIOID REC. = 352, NEUROPEPTIDE-Y REC. = 368; CRF-1 REC. = 307, CRF-1 REC. MUTANT = 307, SOMATOSTATIN-5 REC. = 373, and BOMBESIN-3 REC. = 486. See text for details of each peptide-receptor match and the relevant experiments in chimeric exchanges and point mutations. Note particularly the top two panels on the right that associate the loss of the peptide ligand-matched dominant hydrophobic free energy receptor mode in a nonbinding mutant receptor for ovine corticotropin releasing factor.