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J. Biol. Chem., Vol. 277, Issue 17, 14483-14492, April 26, 2002

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The Chain Length Dependence of Helix Formation of the Second Transmembrane Domain of a G Protein-coupled Receptor of Saccharomyces cerevisiae^*

Fa-Xiang Ding, David Schreiber, Nathan C. VerBerkmoes^§¶, Jeffrey M. Becker^§, and Fred Naider^**

From the  Department of Chemistry, The College of Staten Island of the City University of New York, Staten Island, New York 10314, the ^§ Graduate School of Genome Science and Technology, University of Tennessee-Oak Ridge National Laboratory, Oak Ridge, Tennessee 37830-8026, the ^¶ Organic and Biological Mass Spectrometry Group, Oak Ridge National Laboratory, Oak Ridge, Tennessee 38731-6365, and the  Department of Microbiology and Department of Biochemistry, Cellular and Molecular Biology, University of Tennessee, Knoxville, Tennessee 37996

The chain length dependence of helix formation of transmembrane peptides in lipids was investigated using fragments corresponding to the second transmembrane domain of the -factor receptor from Saccharomyces cerevisiae. Seven peptides with chain lengths of 10 (M2-10; FKYLLSNYSS), 14 (M2-14), 18 (M2-18), 22 (M2-22), 26 (M2-26), 30 (M2-30) and 35 (M2-35; RSRKTPIFIINQVSLFLIILHSALYFKYLLSNYSS) residues, respectively, were synthesized. CD spectra revealed that M2-10 was disordered, and all of the other peptides assumed partially -helical secondary structures in 99% trifluoroethanol (TFE)/H₂O. In 50% TFE/H₂O, M2-30 assumed a -like structure. The other six peptides exhibited the same CD patterns as those found in 99% TFE/H₂O. In 1,2-dimyristoyl-sn-glycero-3-phosphocholine/1,2-dimyristoyl-sn-glycero-3-phospho-rac-(1-glycerol) (4:1 ratio) vesicles, M2-22, M2-26, and M2-35 formed -helical structures, whereas the other peptides formed -like structures. Fourier transform infrared spectroscopy in 1,2-dimyristoyl-sn-glycero-3-phosphocholine/1,2-dimyristoyl-sn-glycero-3-phospho-rac-(1-glycerol) (4:1) multilayers showed that M2-10, M2-14, M2-18, and M2-30 assumed -structures in this environment. Another homologous 30-residue peptide (M2-30B), missing residues SNYSS from the N terminus and extending to RSRKT on the C terminus, was helical in lipid bilayers, suggesting that residues at the termini of transmembrane domains influence their biophysical properties. Attenuated total reflection Fourier transform infrared spectroscopy revealed that M2-22, M2-26, M2-30B, and M2-35 were -helical and oriented at angles of 12°, 13°, 36°, and 34°, respectively, with respect to the multilayer normal. This study showed that chain length must be taken into consideration when using peptides representing single transmembrane domains as surrogates for regions of an intact receptor. Furthermore, this work indicates that the tilt angle and conformation of transmembrane portions of G protein-coupled receptors may be estimated by detailed spectroscopic measurements of single transmembrane peptides.

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				F. Naider, F.-X. Ding, N. C. VerBerkmoes, B. Arshava, and J. M. Becker Synthesis and Biophysical Characterization of a Multidomain Peptide from a Saccharomyces cerevisiae G Protein-coupled Receptor J. Biol. Chem., December 26, 2003; 278(52): 52537 - 52545. [Abstract] [Full Text] [PDF]