Structure and topology of a peptide segment of the 6th transmembrane domain of the \Saccharomyces\ cerevisae alpha-factor receptor in phospholipid bilayers
A detailed analysis of the structure of an 18-residue peptide AQSLLVPSIIFILAYSLK M6(252-269, C252A) in 1,2-dimyristoyl-sn-glycero-phosphocholine bilayers was carried out using solid state NMR and attenuated total reflection Fourier transform infrared spectroscopy. The peptide corresponds to a portion of the 6th transmembrane domain of the alpha-factor receptor of Saccharomyces cerevisiae. Ten homologs of M6(252-269, C252A) were synthesized in which individual residues were labeled with (15)N. One- and two-dimensional solid state NMR experiments were used to determine the chemical shifts and (1)H-(15)N dipolar coupling constants for the (15)N-labeled peptides in oriented dimyristoylphosphatidylcholine bilayers on stacked glass plates. These parameters were used to calculate the structure and orientation of M6(252-269, C252A) in the bilayers. The results indicate that the carboxyl terminal residues (9-14) are alpha-helical and oriented with an angle of about 8 degrees with respect to the bilayer normal. Independently, an attenuated total reflection Fourier transform infrared spectroscopy analysis on M6(252-269, C252A) in a 1,2-dimyristoyl-sn-glycero-phosphocholine bilayer concluded that the helix tilt angle was about 12.5 degrees. The results on the structure of M6(252-269, C252A) in bilayers are in good agreement with the structure determined in trifluoroethanol/water solutions (B. Arshava et al. Biopolymers, 1998, Vol. 46, pp. 343-357). The present study shows that solid state NMR spectroscopy can provide high resolution information on the structure of transmembrane domains of a G protein-coupled receptor.
%0 Journal Article
%1 valentine_structure_2001
%A Valentine, K G
%A Liu, S F
%A Marassi, F M
%A Veglia, G
%A Opella, S J
%A Ding, F X
%A Wang, S H
%A Arshava, B
%A Becker, J M
%A Naider, F
%D 2001
%J Biopolymers
%K Acid Amino Data,Nitrogen Factor,Models,Molecular,Molecular Factors Infrared,Lipid Isotopes,Peptide,Peptides,Phospholipids,Protein Resonance Sequence Sequence,Biopolymers,Fourier Spectroscopy,Mating Structure,Receptors,Saccharomyces Transform bilayers,Magnetic cerevisiae,Spectroscopy,Tertiary,Transcription
%N 4
%P 243--256
%R 10.1002/1097-0282(20011005)59:4<243::AID-BIP1021>3.0.CO;2-H
%T Structure and topology of a peptide segment of the 6th transmembrane domain of the \Saccharomyces\ cerevisae alpha-factor receptor in phospholipid bilayers
%V 59
%X A detailed analysis of the structure of an 18-residue peptide AQSLLVPSIIFILAYSLK M6(252-269, C252A) in 1,2-dimyristoyl-sn-glycero-phosphocholine bilayers was carried out using solid state NMR and attenuated total reflection Fourier transform infrared spectroscopy. The peptide corresponds to a portion of the 6th transmembrane domain of the alpha-factor receptor of Saccharomyces cerevisiae. Ten homologs of M6(252-269, C252A) were synthesized in which individual residues were labeled with (15)N. One- and two-dimensional solid state NMR experiments were used to determine the chemical shifts and (1)H-(15)N dipolar coupling constants for the (15)N-labeled peptides in oriented dimyristoylphosphatidylcholine bilayers on stacked glass plates. These parameters were used to calculate the structure and orientation of M6(252-269, C252A) in the bilayers. The results indicate that the carboxyl terminal residues (9-14) are alpha-helical and oriented with an angle of about 8 degrees with respect to the bilayer normal. Independently, an attenuated total reflection Fourier transform infrared spectroscopy analysis on M6(252-269, C252A) in a 1,2-dimyristoyl-sn-glycero-phosphocholine bilayer concluded that the helix tilt angle was about 12.5 degrees. The results on the structure of M6(252-269, C252A) in bilayers are in good agreement with the structure determined in trifluoroethanol/water solutions (B. Arshava et al. Biopolymers, 1998, Vol. 46, pp. 343-357). The present study shows that solid state NMR spectroscopy can provide high resolution information on the structure of transmembrane domains of a G protein-coupled receptor.
@article{valentine_structure_2001,
abstract = {A detailed analysis of the structure of an 18-residue peptide AQSLLVPSIIFILAYSLK [M6(252-269, C252A)] in 1,2-dimyristoyl-sn-glycero-phosphocholine bilayers was carried out using solid state NMR and attenuated total reflection Fourier transform infrared spectroscopy. The peptide corresponds to a portion of the 6th transmembrane domain of the alpha-factor receptor of Saccharomyces cerevisiae. Ten homologs of M6(252-269, C252A) were synthesized in which individual residues were labeled with (15)N. One- and two-dimensional solid state NMR experiments were used to determine the chemical shifts and (1)H-(15)N dipolar coupling constants for the (15)N-labeled peptides in oriented dimyristoylphosphatidylcholine bilayers on stacked glass plates. These parameters were used to calculate the structure and orientation of M6(252-269, C252A) in the bilayers. The results indicate that the carboxyl terminal residues (9-14) are alpha-helical and oriented with an angle of about 8 degrees with respect to the bilayer normal. Independently, an attenuated total reflection Fourier transform infrared spectroscopy analysis on M6(252-269, C252A) in a 1,2-dimyristoyl-sn-glycero-phosphocholine bilayer concluded that the helix tilt angle was about 12.5 degrees. The results on the structure of M6(252-269, C252A) in bilayers are in good agreement with the structure determined in trifluoroethanol/water solutions (B. Arshava et al. Biopolymers, 1998, Vol. 46, pp. 343-357). The present study shows that solid state NMR spectroscopy can provide high resolution information on the structure of transmembrane domains of a G protein-coupled receptor.},
added-at = {2017-03-14T02:48:56.000+0100},
author = {Valentine, K G and Liu, S F and Marassi, F M and Veglia, G and Opella, S J and Ding, F X and Wang, S H and Arshava, B and Becker, J M and Naider, F},
biburl = {https://www.bibsonomy.org/bibtex/2d47b6f448af162692af2c2e9d4cbc21c/nmrresource},
doi = {10.1002/1097-0282(20011005)59:4<243::AID-BIP1021>3.0.CO;2-H},
interhash = {052403858e020ceda0cf5aa91bc922c9},
intrahash = {d47b6f448af162692af2c2e9d4cbc21c},
issn = {0006-3525},
journal = {Biopolymers},
keywords = {Acid Amino Data,Nitrogen Factor,Models,Molecular,Molecular Factors Infrared,Lipid Isotopes,Peptide,Peptides,Phospholipids,Protein Resonance Sequence Sequence,Biopolymers,Fourier Spectroscopy,Mating Structure,Receptors,Saccharomyces Transform bilayers,Magnetic cerevisiae,Spectroscopy,Tertiary,Transcription},
month = oct,
number = 4,
pages = {243--256},
pmid = {11473349},
timestamp = {2017-03-14T02:49:21.000+0100},
title = {{Structure and topology of a peptide segment of the 6th transmembrane domain of the {\{}Saccharomyces{\}} cerevisae alpha-factor receptor in phospholipid bilayers}},
volume = 59,
year = 2001
}