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. 1985 Dec;48(6):873–876. doi: 10.1016/S0006-3495(85)83848-0

Further Characterization of Protein Secondary Structures in Purple Membrane by Circular Dichroism and Polarized Infrared Spectroscopies

E Nabedryk, A M Bardin, J Breton
PMCID: PMC1329418  PMID: 19431599

Abstract

The conformation and the orientation of the protein secondary structures in purple membrane was analyzed by infrared absorption and linear dichroism of oriented membranes as well as by UV circular dichroism of bacteriorhodopsin in intact purple membrane and in lipid vesicles. A large amount (74 ± 5%) of transmembrane α-helices is detected with no significant contribution of β-sheet strands running perpendicular to the membrane plane. Thus, these data do not support the recent structural model proposed by Jap et al. (Biophys. J. 1983, 43:81-89).

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bandekar J., Krimm S. Vibrational analysis of peptides, polypeptides, and proteins: Characteristic amide bands of beta-turns. Proc Natl Acad Sci U S A. 1979 Feb;76(2):774–777. doi: 10.1073/pnas.76.2.774. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Becher B., Cassim J. Y. Effects of light adaptation on the purple membrane structure of Halobacterium halobium. Biophys J. 1976 Oct;16(10):1183–1200. doi: 10.1016/S0006-3495(76)85767-0. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Chen Y. H., Yang J. T., Chau K. H. Determination of the helix and beta form of proteins in aqueous solution by circular dichroism. Biochemistry. 1974 Jul 30;13(16):3350–3359. doi: 10.1021/bi00713a027. [DOI] [PubMed] [Google Scholar]
  4. Chou P. Y., Fasman G. D. Beta-turns in proteins. J Mol Biol. 1977 Sep 15;115(2):135–175. doi: 10.1016/0022-2836(77)90094-8. [DOI] [PubMed] [Google Scholar]
  5. Engelman D. M., Henderson R., McLachlan A. D., Wallace B. A. Path of the polypeptide in bacteriorhodopsin. Proc Natl Acad Sci U S A. 1980 Apr;77(4):2023–2027. doi: 10.1073/pnas.77.4.2023. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Hayward S. B., Stroud R. M. Projected structure of purple membrane determined to 3.7 A resolution by low temperature electron microscopy. J Mol Biol. 1981 Sep 25;151(3):491–517. doi: 10.1016/0022-2836(81)90007-3. [DOI] [PubMed] [Google Scholar]
  7. Henderson R. The structure of the purple membrane from Halobacterium hallobium: analysis of the X-ray diffraction pattern. J Mol Biol. 1975 Apr 5;93(2):123–138. doi: 10.1016/0022-2836(75)90123-0. [DOI] [PubMed] [Google Scholar]
  8. Henderson R., Unwin P. N. Three-dimensional model of purple membrane obtained by electron microscopy. Nature. 1975 Sep 4;257(5521):28–32. doi: 10.1038/257028a0. [DOI] [PubMed] [Google Scholar]
  9. Jap B. K., Maestre M. F., Hayward S. B., Glaeser R. M. Peptide-chain secondary structure of bacteriorhodopsin. Biophys J. 1983 Jul;43(1):81–89. doi: 10.1016/S0006-3495(83)84326-4. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Leifer D., Henderson R. Three-dimensional structure of orthorhombic purple membrane at 6.5 A resolution. J Mol Biol. 1983 Jan 25;163(3):451–466. doi: 10.1016/0022-2836(83)90068-2. [DOI] [PubMed] [Google Scholar]
  11. Long M. M., Urry D. W., Stoeckenius W. Circular dichroism of biological membranes: purple membrane of Halobacterium halobium. Biochem Biophys Res Commun. 1977 Apr 11;75(3):725–731. doi: 10.1016/0006-291x(77)91532-7. [DOI] [PubMed] [Google Scholar]
  12. Mao D., Wachter E., Wallace B. A. Folding of the mitochondrial proton adenosinetriphosphatase proteolipid channel in phospholipid vesicles. Biochemistry. 1982 Sep 28;21(20):4960–4968. doi: 10.1021/bi00263a020. [DOI] [PubMed] [Google Scholar]
  13. Mao D., Wallace B. A. Differential light scattering and absorption flattening optical effects are minimal in the circular dichroism spectra of small unilamellar vesicles. Biochemistry. 1984 Jun 5;23(12):2667–2673. doi: 10.1021/bi00307a020. [DOI] [PubMed] [Google Scholar]
  14. Nabedryk E., Breton J. Orientation of intrinsic proteins in photosynthetic membranes. Polarized infrared spectroscopy of chloroplasts and chromatophores. Biochim Biophys Acta. 1981 May 13;635(3):515–524. doi: 10.1016/0005-2728(81)90110-9. [DOI] [PubMed] [Google Scholar]
  15. Rothschild K. J., Clark N. A. Polarized infrared spectroscopy of oriented purple membrane. Biophys J. 1979 Mar;25(3):473–487. doi: 10.1016/S0006-3495(79)85317-5. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Trewhella J., Anderson S., Fox R., Gogol E., Khan S., Engelman D., Zaccai G. Assignment of segments of the bacteriorhodopsin sequence to positions in the structural map. Biophys J. 1983 Jun;42(3):233–241. doi: 10.1016/S0006-3495(83)84391-4. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Wallace B. A., Henderson R. Location of the carboxyl terminus of bacteriorhodopsin in purple membrane. Biophys J. 1982 Sep;39(3):233–239. doi: 10.1016/S0006-3495(82)84513-X. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Wallace B. A., Kohl N. The C-terminus of bacteriorhodopsin is a random coil. Biochim Biophys Acta. 1984 Oct 17;777(1):93–98. doi: 10.1016/0005-2736(84)90500-5. [DOI] [PubMed] [Google Scholar]
  19. Wallace B. A., Mao D. Circular dichroism analyses of membrane proteins: an examination of differential light scattering and absorption flattening effects in large membrane vesicles and membrane sheets. Anal Biochem. 1984 Nov 1;142(2):317–328. doi: 10.1016/0003-2697(84)90471-8. [DOI] [PubMed] [Google Scholar]
  20. Wu C. S., Hachimori A., Yang J. T. Lipid-induced ordered conformation of some peptide hormones and bioactive oligopeptides: predominance of helix over beta form. Biochemistry. 1982 Sep 14;21(19):4556–4562. doi: 10.1021/bi00262a007. [DOI] [PubMed] [Google Scholar]

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