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Synthetic peptides as probes for conformational preferences of domains of membrane receptors
Author(s) -
Naider Fred,
Khare Sanjay,
Arshava Boris,
Severino Beatrice,
Russo Joe,
Becker Jeffrey M.
Publication year - 2004
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.20183
Subject(s) - chemistry , transmembrane domain , peptide , transmembrane protein , micelle , receptor , stereochemistry , biophysics , biochemistry , aqueous solution , organic chemistry , biology
Peptide models have been widely used to investigate conformational aspects of domains of proteins since the early 1950s. A pioneer in this field was Dr. Murray Goodman, who applied a battery of methodologies to study the onset of structure in homooligopeptides. This article reviews some of Dr. Goodman's contributions, and reports recent studies using linear and constrained peptides corresponding to the first extracellular loop and linear peptides corresponding to the sixth transmembrane domain of a G‐protein coupled receptor from the yeast Saccharomyces cerevisiae . Peptides containing 30–40 residues were synthesized using solid‐phase methods and purified to near homogeneity by reversed phase high performance liquid chromatography. CD and NMR analyses indicated that the first extracellular loop peptides were mostly flexible in water, and assumed some helical structure near the N‐terminus in trifluoroethanol and in the presence of micelles. Comparison of oligolysines with native loop residues revealed that three lysines at each terminus of a peptide corresponding to the sixth transmembrane domain of the α‐factor receptor resulted in better aqueous solubility and greater helicity than the native loop residues. © 2004 Wiley Periodicals, Inc. Biopolymers (Pept Sci), 2005