Secondary Structure of the Exchange-Resistant Core from the Nicotinic Acetylcholine Receptor Probed Directly by Infrared Spectroscopy and Hydrogen/Deuterium Exchange
The spectral changes that occur in infrared spectra recorded as a function of time after exposure of the nicotinic acetylcholine receptor (nAChR) to 2H2O buffer were examined in order to investigate the secondary structure of the transmembrane domain. The resolution-enhanced amide I band in spectra...
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Published in | Biochemistry (Easton) Vol. 37; no. 42; pp. 14815 - 14822 |
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Main Authors | , |
Format | Journal Article |
Language | English |
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United States
American Chemical Society
20.10.1998
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Abstract | The spectral changes that occur in infrared spectra recorded as a function of time after exposure of the nicotinic acetylcholine receptor (nAChR) to 2H2O buffer were examined in order to investigate the secondary structure of the transmembrane domain. The resolution-enhanced amide I band in spectra recorded during the first 12 h after exposure to 2H2O exhibits subtle downshifts in frequency of α-helical and β-sheet vibrations. A strong intensity of the unexchanged α-helical vibration near 1655 cm-1 after 3 days exposure to 2H2O suggests that a large proportion of the remaining 25% of unexchanged peptide hydrogens adopts an α-helical conformation. Further exposure of the nAChR to 2H2O under conditions of both increasing pH and membrane “fluidity” led to additional exchange of peptide hydrogens for deuterium. The greatest degree of peptide 1H/2H exchange (95%) under nondenaturing conditions was found for the nAChR reconstituted into the highly fluid egg phosphatidylcholine membranes lacking cholesterol and anionic lipids at pH 9.0. This enhanced exchange was accompanied by a decrease in intensity near 1655 cm-1 due to the downshift in frequency of peptides in the α-helical conformation, whereas no clear evidence was found for the further exchange of β-sheet. Some unexchanged α-helical peptide hydrogens were still observed. As the exchange-resistant peptides likely include those found within the hydrophobic environment of the lipid bilayer, these data strongly support an α-helical secondary structure of the transmembrane domain. |
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AbstractList | The spectral changes that occur in infrared spectra recorded as a function of time after exposure of the nicotinic acetylcholine receptor (nAChR) to 2H2O buffer were examined in order to investigate the secondary structure of the transmembrane domain. The resolution-enhanced amide I band in spectra recorded during the first 12 h after exposure to 2H2O exhibits subtle downshifts in frequency of α-helical and β-sheet vibrations. A strong intensity of the unexchanged α-helical vibration near 1655 cm-1 after 3 days exposure to 2H2O suggests that a large proportion of the remaining 25% of unexchanged peptide hydrogens adopts an α-helical conformation. Further exposure of the nAChR to 2H2O under conditions of both increasing pH and membrane “fluidity” led to additional exchange of peptide hydrogens for deuterium. The greatest degree of peptide 1H/2H exchange (95%) under nondenaturing conditions was found for the nAChR reconstituted into the highly fluid egg phosphatidylcholine membranes lacking cholesterol and anionic lipids at pH 9.0. This enhanced exchange was accompanied by a decrease in intensity near 1655 cm-1 due to the downshift in frequency of peptides in the α-helical conformation, whereas no clear evidence was found for the further exchange of β-sheet. Some unexchanged α-helical peptide hydrogens were still observed. As the exchange-resistant peptides likely include those found within the hydrophobic environment of the lipid bilayer, these data strongly support an α-helical secondary structure of the transmembrane domain. The spectral changes that occur in infrared spectra recorded as a function of time after exposure of the nicotinic acetylcholine receptor (nAChR) to 2H2O buffer were examined in order to investigate the secondary structure of the transmembrane domain. The resolution-enhanced amide I band in spectra recorded during the first 12 h after exposure to 2H2O exhibits subtle downshifts in frequency of alpha-helical and beta-sheet vibrations. A strong intensity of the unexchanged alpha-helical vibration near 1655 cm-1 after 3 days exposure to 2H2O suggests that a large proportion of the remaining 25% of unexchanged peptide hydrogens adopts an alpha-helical conformation. Further exposure of the nAChR to 2H2O under conditions of both increasing pH and membrane "fluidity" led to additional exchange of peptide hydrogens for deuterium. The greatest degree of peptide 1H/2H exchange (95%) under nondenaturing conditions was found for the nAChR reconstituted into the highly fluid egg phosphatidylcholine membranes lacking cholesterol and anionic lipids at pH 9.0. This enhanced exchange was accompanied by a decrease in intensity near 1655 cm-1 due to the downshift in frequency of peptides in the alpha-helical conformation, whereas no clear evidence was found for the further exchange of beta-sheet. Some unexchanged alpha-helical peptide hydrogens were still observed. As the exchange-resistant peptides likely include those found within the hydrophobic environment of the lipid bilayer, these data strongly support an alpha-helical secondary structure of the transmembrane domain. The spectral changes that occur in infrared spectra recorded as a function of time after exposure of the nicotinic acetylcholine receptor (nAChR) to super(2)H sub(2)O buffer were examined in order to investigate the secondary structure of the transmembrane domain. The resolution-enhanced amide I band in spectra recorded during the first 12 h after exposure to super(2)H sub(2)O exhibits subtle downshifts in frequency of alpha -helical and beta -sheet vibrations. A strong intensity of the unexchanged alpha -helical vibration near 1655 cm super(-1) after 3 days exposure to super(2)H sub(2)O suggests that a large proportion of the remaining 25% of unexchanged peptide hydrogens adopts an alpha -helical conformation. Further exposure of the nAChR to super(2)H sub(2)O under conditions of both increasing pH and membrane "fluidity" led to additional exchange of peptide hydrogens for deuterium. The greatest degree of peptide super(1)H/ super(2)H exchange (95%) under nondenaturing conditions was found for the nAChR reconstituted into the highly fluid egg phosphatidylcholine membranes lacking cholesterol and anionic lipids at pH 9.0. This enhanced exchange was accompanied by a decrease in intensity near 1655 cm super(-1) due to the downshift in frequency of peptides in the alpha -helical conformation, whereas no clear evidence was found for the further exchange of beta -sheet. Some unexchanged alpha -helical peptide hydrogens were still observed. As the exchange-resistant peptides likely include those found within the hydrophobic environment of the lipid bilayer, these data strongly support an alpha -helical secondary structure of the transmembrane domain. |
Author | Baenziger, John E Méthot, Nathalie |
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Cites_doi | 10.1038/373037a0 10.1007/BF01877228 10.1016/0014-5793(87)80191-6 10.1021/j100830a521 10.1021/bi00383a003 10.1074/jbc.270.49.29129 10.1016/0014-5793(77)80496-1 10.1111/j.1432-1033.1996.0539u.x 10.1146/annurev.bi.41.070172.004351 10.3109/10409239509085140 10.1016/S0021-9258(18)99381-6 10.1016/0167-4838(89)90075-7 10.1002/j.1460-2075.1985.tb03821.x 10.1111/j.1432-1033.1995.0839a.x 10.1038/353846a0 10.1006/jmbi.1993.1107 10.1016/S0021-9258(17)35695-8 10.1074/jbc.273.2.771 10.1016/0896-6273(90)90445-L 10.1016/0003-9861(87)90319-5 10.1016/0022-2836(75)90123-0 10.1093/protein/9.1.51 10.1002/j.1460-2075.1994.tb06266.x 10.1016/0167-4838(86)90024-5 10.1016/0167-4838(86)90314-6 |
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Notes | ark:/67375/TPS-K3NHLGHC-5 istex:39315B687424BA1FC60CC080D1F8F5A647E210BD This work was supported by a grant from the Medical Council of Canada to J.E.B. and by a doctoral scholarship from the Natural Sciences and Engineering Research Council to N.M. ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
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Snippet | The spectral changes that occur in infrared spectra recorded as a function of time after exposure of the nicotinic acetylcholine receptor (nAChR) to 2H2O... The spectral changes that occur in infrared spectra recorded as a function of time after exposure of the nicotinic acetylcholine receptor (nAChR) to super(2)H... |
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SubjectTerms | Amides Animals Deuterium Oxide Hydrogen Hydrogen-Ion Concentration Peptides - chemistry Phosphatidylcholines Phospholipids Protein Denaturation Protein Structure, Secondary Receptor, Muscarinic M1 Receptor, Muscarinic M4 Receptors, Muscarinic - chemistry Receptors, Nicotinic - chemistry Spectroscopy, Fourier Transform Infrared Temperature Torpedo |
Title | Secondary Structure of the Exchange-Resistant Core from the Nicotinic Acetylcholine Receptor Probed Directly by Infrared Spectroscopy and Hydrogen/Deuterium Exchange |
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