NMR and circular dichroism studies of synthetic peptides derived from the third intracellular loop of the beta-adrenoceptor.
The C-terminal part of the third intracellular loop of the beta-adrenoceptor is capable of stimulating adenylate cyclase in the presence of phospholipid vesicles via the stimulatory guanine nucleotide binding protein (Gs) [Palm et al. (1989) FEBS Lett. 254, 89-93]. We have investigated the structure of synthetic peptides corresponding to residues 284-295 of the turkey erythrocyte adrenoceptor in micelles, trifluoroethanol and aqueous solution, by using 2D 1H NMR and CD. In the presence of phospholipid micelles the peptides display a C-terminal alpha-helical region, whereas the N-terminal part was found to be highly flexible.
Jung
H
H
Theodor-Boveri-Institut für Biowissenschaften, Universität Würzburg, Germany.
Windhaber
R
R
Palm
D
D
Schnackerz
K D
KD
D000595:Amino Acid Sequence; D000818:Animals; D002942:Circular Dichroism; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000138:chemical synthesis / Q000737:chemistry; D011487:Protein Conformation; D011943:Receptors, Adrenergic, beta / Q000737:chemistry*; D014270:Trifluoroethanol / Q000737:chemistry; D014422:Turkeys
D010446:Peptide Fragments; D011943:Receptors, Adrenergic, beta; D014270:Trifluoroethanol