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NMR and circular dichroism studies of synthetic peptides derived from the third intracellular loop of the β‐adrenoceptor
Author(s) -
Jung Hans,
Windhaber Ralf,
Palm Dieter,
Schnackerz Klaus D.
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)01409-t
Subject(s) - circular dichroism , chemistry , micelle , adenylate kinase , phospholipid , intracellular , nucleotide , vesicle , cyclase , peptide , stereochemistry , guanine , biochemistry , aqueous solution , membrane , enzyme , organic chemistry , gene
The C‐terminal part of the third intracellular loop of the β‐adrenoceptor is capable of stimulating adenylate cyclase in the presence of phospholipid vesicles via the stimulatory guanine nucleotide binding protein (G s ) [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 1 H NMR and CD. In the presence of phospholipid micelles the peptides display a C‐terminal α‐helical region, whereas the N‐terminal part was found to be highly flexible.