Skip to main content
SpringerLink
Log in

Absorption and Optical Rotation Spectra of Biological Membranes

Distortions and Their Corrections

  • Chapter
Physiology of Membrane Disorders

  • 270 Accesses

Abstract

The combination of ultraviolet absorption and circular dichroism (CD) spectroscopies provides a sensitive technique for following protein conformation and conformational changes in solution. It is reasonable to predict that the application of these methods to the study of biomembrane protein structure should yield valuable information about their averaged conformation and changes that might occur with changes in functional state. And indeed they do, after and only after appropriate data analyses, for the particulate nature of membranes gives rise to correctable scattering artifacts. In considering the CD spectrum of membranes, the objective is to eliminate the distortions due to their particulate nature by correcting the spectrum to the absorbance or difference absorbance values that would have occurred had the membrane proteins been molecularly dispersed in a state conformationally equivalent to that in the membrane. The corrected CD spectrum is then compared to reference spectra to estimate the average structure and/or compared to spectra of the membrane in different functional states to follow possible conformational changes. If a membrane suspension is challenged, for example, by the addition of substrate for one of the membrane-bound enzymes, and a difference in its CD spectrum is observed, this cannot be judged to be real until the scattering problem has been properly analyzed. This is not an onerous task, and indeed is straightforward, in large measure due to the arguments and methods known as the pseudoreference state (prs) approach described in detail in 1972(1) but whose origins go back to 1968. (2) This chapter will consider first absorption spectroscopy and then the related phenomenon of CD and its dispersion counterpart, optical rotatory dispersion, for both solutions and suspensions. The corrected spectra of the purple membrane provide a sample calculation demonstrating an application of the prs approach.

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Log in via an institution
Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 74.99
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Urry, D. W. 1972. Protein conformation in biomembranes: Optical rotation and absorption of membrane suspensions. Biochim. Biophys. Acta 265: 115–168.

    PubMed  CAS  Google Scholar 

  2. Urry, D. W., andT. H. Ji. 1968. Distortions in circular dichroism patterns of particulate (or membranous) systems. Arch. Biochem. Biophys. 128: 802–807.

    PubMed  CAS  Google Scholar 

  3. Moscowitz, A. 1960. Theory and analysis of rotatory dispersion curves. In: Optical Rotatory Dispersion. C. Djerassi, ed. McGraw-Hill, New York. pp. 150–177.

    Google Scholar 

  4. Urry, D. W. 1970. Spectroscopic Approaches to Biomolecular Conformation. AMA Press, Chicago, pp. 33–121.

    Google Scholar 

  5. Kasha, M. 1963. Energy transfer mechanisms and the molecular exciton model for molecular aggregates. Radiat. Res. 20: 55–71.

    PubMed  CAS  Google Scholar 

  6. Rhodes, W. 1961. The hypochromism and other spectral properties of helical polynucleotides. J. Am. Chem. Soc. 83: 3609–3617.

    CAS  Google Scholar 

  7. Tinoco, I., Jr. 1961. Hypochromism in polynucleotides. J. Am. Chem. Soc. 82:4785–4790. Optical and other electronic properties of polymers. J. Chem. Phys. 34: 1067.

    Google Scholar 

  8. Urry, D. W. 1973. Determining biomolecular conformations. III. Ultraviolet absorption spectroscopy. Res. Dev. 24: 28–36.

    Google Scholar 

  9. Quadrifoglio, F., and D. W. Urry. 1968. Ultraviolet rotatory properties of polypeptides in solution. I. Helical poly-L-alanine. J. Am. Chem. Soc. 90: 2755–2760.

    PubMed  CAS  Google Scholar 

  10. Urry, D. W., M. M. Long, T. Ohnishi, and M. Jacobs. 1974. Circular dichroism absorption of the polytetrapeptide of elastin: A polymer model for the P-turn. Biochem. Biophys. Res. Commun. 61: 1427–1433.

    PubMed  CAS  Google Scholar 

  11. Urry, D. W., and M. M. Long. 1974. Circular dichroism and absorption studies on biomembranes. In: Methods in Membrane Biology. E. D. Korn, ed. Plenum Press, New York. pp. 105–141.

    Google Scholar 

  12. Plaschina, I. G., E. E. Braudo, and V. R. Tolstoguzov. 1978. Circular dichroism studies of pectin solutions. Carbohydr. Res. 60: 1–8.

    CAS  Google Scholar 

  13. Homer, R. B., and K. Roberts. 1979. Glycoprotein conformation in plant cell walls. Planta 146: 217–222.

    CAS  Google Scholar 

  14. Gelman, R. A., and J. Blackwell. 1973. Heparin polypeptide interactions in aqueous solution. Arch. Biochem. Biophys. 159: 427–433.

    PubMed  CAS  Google Scholar 

  15. Gelman, R. A., and J. Blackwell. 1975. Interactions between mucopolysaccharides and cationic polypeptides in aqueous solution: Chondroitin 4-sulfate and dermatin sulfate. Biopolymers 12: 1959–1974.

    Google Scholar 

  16. Blackwell, J., K. P. Schodt, and R. A. Gelman. 1977. Polysac¬charide-polypeptide systems as models for heparin interactions. Fed. Proc. 36: 98–101.

    PubMed  CAS  Google Scholar 

  17. Schodt, K. P., and J. Blackwell. 1976. Comparison of four proteoglycans in terms of their interactions with poly (L-arginine). Biopolymers 15: 469–482.

    PubMed  CAS  Google Scholar 

  18. Williams, R. E., P. F. Lurquin, and V. L. Seligy. 1972. Circular dichroism of avian-erythrocyte chromatin and ethidium bromide bound to chromatin. Eur. J. Biochem. 29: 426–432.

    PubMed  CAS  Google Scholar 

  19. Spelsberg, T. C., W. M. Mitchell, andF. Chytil. 1973. Structural alterations of acidic proteins by acid treatment of chromatin. Mol. Cell. Biochem. 1: 243–246.

    PubMed  CAS  Google Scholar 

  20. Burnotte, J., B. D. Stollar, andG. D. Fasman. 1973. Immunological and circular dichroism studies of maleylated f. 1 (A) histone and complexes with DNA. Arch. Biochem. Biophys. 155: 428–435.

    PubMed  CAS  Google Scholar 

  21. Uchiumi, T., A. Hachimori, T. Atsushi, andT. Samejima. 1978. Studies on the negative circular dichroism bands around 297 nm of ribosomes from bacterial cells. Biochim. Biophys. Acta 519: 513–525.

    PubMed  CAS  Google Scholar 

  22. Schooley, R. E., and Govindjee. 1976. Cation-induced changes in the circular dichroism spectrum of chloroplasts. FEBS Lett. 65: 123–125.

    CAS  Google Scholar 

  23. Gross, E. L., and J. Grenier. 1978. Regulation of excitation energy distribution in subchloroplast particles: Photosystem 1. Arch. Biochem. Biophys. 187: 387–398.

    PubMed  CAS  Google Scholar 

  24. Brody, M., and B. Nathanson. 1972. Direct and indirect mecha¬nisms of deaggregation by fatty acids in chlorophyll-containing systems. Biophys. J. 12: 774–790.

    PubMed  CAS  Google Scholar 

  25. Mita, K., S. Ichimura, and M. Zama. 1978. Conformation of poly (L-arginine). II. Complexes with poly anions. Biopolymers 17: 2783–2798.

    CAS  Google Scholar 

  26. Saudek, V., S. Strokrova, and P. Schmidt. 1982. Conformational study of poly (a-L-aspartic acid). Biopolymers 21: 1011–1020.

    CAS  Google Scholar 

  27. Mattice, W. L., and W. H. Hanison. 1976. The importance of coulombic interactions for the induction of p structure in lysine oligomers by sodium dodecyl sulfate. Biopolymers 15: 559–567.

    PubMed  CAS  Google Scholar 

  28. Ernst, C., J. Grange, H. Rinnert, G. DuPont, and J. LeMatre. 1981. Structure of amphotericin B aggregates as revealed by UV and CD spectroscopies. Biopolymers 20: 1575–1588.

    CAS  Google Scholar 

  29. Siezen, R. J., and J. G. Bindels. 1982. Stepwise dissocia-tion/denaturation and reassociation/renaturation of bovine a- crystallin in urea and guanidine hydrochloride: Sedimentation, fluorescence, near-ultraviolet and far-ultraviolet circular dichroism studies. Exp. Eye Res. 34: 969–983.

    PubMed  CAS  Google Scholar 

  30. Strom, R., C. Crifo, V. Viti, L. Guidoni, and F. Podo. 1978. Variations in CD and H-NMR relaxation properties of melittin upon interaction with phospholipids. FEBS Lett. 96: 45–50.

    PubMed  CAS  Google Scholar 

  31. Drake, A. F., and R. C. Hider. 1979. The structure of melittin in lipid bilayer membranes. Biochim. Biophys. Acta 555: 371–373.

    PubMed  CAS  Google Scholar 

  32. Yu, K.-Y., J. J. Baldassare, and C. Ho. 1974. Physical chemical studies of phospholipids and poly(amino acids) interactions. Biochemistry 13: 4375 - 4381.

    PubMed  CAS  Google Scholar 

  33. Wulf, J., and W. G. Pohl. 1977. Calcium ion flux across phosphatidylcholine membranes mediated by ionophore A23187. Biochim. Biophys. Acta 465: 471–485.

    PubMed  CAS  Google Scholar 

  34. Khare, R. S., R. K. Mishra, W. H. Falor, and A. J. Hopfinger. 1974. The circular dichroism of sphingomyelin. Curr. Sci. 43: 67–71.

    CAS  Google Scholar 

  35. Khare, R. S. 1975. X-ray, electron and optical studies on membrane drug interactions. Stud. Biophys. 48: 161–172.

    CAS  Google Scholar 

  36. Khare, R. S., R. K. Mishra, and W. H. Falor. 1976. Influence of psychoactive drugs on the circular dichroism spectra of lyotropic dispersions of sphingomyelin. Indian J. Biochem. Biophys. 11: 331–334.

    Google Scholar 

  37. McMillin, C. R., and A. G. Walton. 1974. A circular dichroism technique for the study of adsorbed protein structure. J. Colloid Interface Sci. 48: 345–349.

    CAS  Google Scholar 

  38. Ji, T. H. 1973. Circular dichroism of a membrane protein of Neurospora crassa. Biochem. Biophys. Res. Commun. 51: 829–835.

    PubMed  CAS  Google Scholar 

  39. Braun, V. 1975. Covalent lipoprotein from the outer membrane of Escherichia coli. Biochim. Biophys. Acta 415: 335–377.

    PubMed  CAS  Google Scholar 

  40. Andreu, J., and E. Munoz. 1979. Molecular properties of random coil and refolded forms of a and (3 subunits of an energy transducing ATPase from bacterial membranes. Biochemistry 18: 1836–1844.

    PubMed  CAS  Google Scholar 

  41. Long, M. M., D. W. Urry, and W. Stoeckenius. 1977. Circular dichroism of biological membranes: Purple membrane of Halobacterium halobium. Biochem. Biophys. Res. Commun. 75: 725–731.

    PubMed  CAS  Google Scholar 

  42. Urry, D. W., and M. M. Long. 1978. Ultraviolet absorption, circular dichroism, and optical rotatory dispersion in biomembrane studies. In: Physiology of Membrane Disorders. T. E. Andreoli, J. F. Hoffman, and D. D. Fanestil, eds. Plenum Press, New York. pp. 107–124.

    Google Scholar 

  43. Brith-Lindner, M., and K. Rosenheck. 1977. The circular dichroism of bacteriorhodopsin: Asymmetry and light scattering distortions. FEBS Lett. 76: 41–44.

    CAS  Google Scholar 

  44. Papahadopoulos, G. K., D. D. Muccio, T. L. Hsiao, and J. Y. Cassim. 1978. Comparative studies on the fine structure of purple membrane from Halobacterium cutirubrum and Halobacterium halobium. J. Membr. Biol. 43: 277–294.

    Google Scholar 

  45. Muccio, D. D., and J. Y. Cassim. 1979. Interpretations of the effects of pH on the spectra of purple membrane. J. Mol. Biol. 135: 595–609.

    PubMed  CAS  Google Scholar 

  46. Ji, T. H., and D. W. Urry. 1969. Correlation of light scattering and absorption flattening effects with distortions in the circular dichroism patterns of mitochondrial membrane fragments. Biochem. Biophys. Res. Commun. 34: 404–411.

    PubMed  CAS  Google Scholar 

  47. Urry, D. W., L. Masotti, and J. Krivacic. 1970. Improved ellipticity data for several biological membranes. Biochem. Biophys. Res. Commun. 41: 521–524.

    PubMed  CAS  Google Scholar 

  48. Urry, D. W., L. Masotti, and J. R. Krivacic. 1971. Circular dichroism of biological membranes. I. Mitochondria and red blood cell ghosts. Biochim. Biophys. Acta 241: 600–612.

    PubMed  CAS  Google Scholar 

  49. Masotti, L., G. Lenaz, A. Spisni, andD. W. Urry. 1974. Effect of phospholipids on the protein conformation in the inner mitochondrial membranes. Biochem. Biophys. Res. Commun. 56: 892–897.

    PubMed  CAS  Google Scholar 

  50. Storey, B. T., and C. P. Lee. 1973. Circular dichroism of cytochrome oxidase, cytochrome b566, and cytochrome c in beef heart mitochondrial membrane fragments. Biochim. Biophys. Acta 292: 554–565.

    PubMed  CAS  Google Scholar 

  51. Arutjunjan, A. M., A. A. Konstantinov, and Y. A. Sharonor. 1974. Magnetic circular dichroism and magnetooptical rotatory dispersion of submitochondrial particles at room and liquid nitrogen temperatures. FEBS Lett. 46: 317–320.

    PubMed  CAS  Google Scholar 

  52. Masotti, L., D. W. Urry, and R. Llinas. 1973. Circular dichroism of lobster axonal membranes. Acta Vitaminol. Enzymol. 27: 154–158.

    PubMed  CAS  Google Scholar 

  53. Long, M. M., L. Masotti, G. Sachs, and D. W. Urry. 1973. Circular dichroism of biological membranes-brain microsomes. J. Supramol. Struct. 1: 259–268.

    PubMed  CAS  Google Scholar 

  54. Long, M. M., and D. W. Urry. 1981. Absorption and circular dichroism spectroscopies. In: Membrane Spectroscopy. E. Grell, ed. Springer-Verlag, Berlin, pp. 143–171.

    Google Scholar 

  55. Kornguth, S. E., A. Flangas, J. Perrin, R. Geison, and G. Scott. 1972. Isolation of synaptic complexes in a CsCl gradient: Conditions for maximal resolution in the zonal rotor B-XIV and circular dichroism patterns. Prep. Biochem. 2: 167–192.

    PubMed  CAS  Google Scholar 

  56. Saccomani, G., J. G. Spenney, D. W. Urry, andG. Sachs. 1974. Preparation and characterization of plasma membrane of cardiac tissue. J. Mol. Cell. Cardiol. 6: 505–521.

    PubMed  CAS  Google Scholar 

  57. Masotti, L., M. M. Long, G. Sachs, and D. W. Urry. 1972. The effect of ATP on the CD spectrum of membrane fraction from oxyntic cells. Biochim. Biophys. Acta 255: 420–424.

    PubMed  CAS  Google Scholar 

  58. Masotti, L., D. W. Urry, J. R. Krivacic, and M. M. Long. 1972. Circular dichroism of biological membranes. II. Plasma membranes and sarcotubular vesicles. Biochim. Biophys. Acta 266: 7–17.

    PubMed  CAS  Google Scholar 

  59. Reinert, J. C., and L. J. Davis. 1971. The circular dichroism spectrum of microsomal membranes: Magnesium induced aggregation. Biochim. Biophys. Acta 241: 921–924.

    PubMed  CAS  Google Scholar 

  60. Rubin, M. S., N. J. Swislocki, and M. Schenberg. 1973. Alteration of liver plasma membrane protein conformation by bovine growth hormone in vitro. Arch. Biochem. Biophys. 157: 252–259.

    PubMed  CAS  Google Scholar 

  61. Schneider, A. S., M.-J.T. Schneider, and K. Rosenheck. 1970. Optical activity of biological membranes: Scattering effects and protein conformations. Proc. Natl. Acad. Sci. USA 66: 793–798.

    PubMed  CAS  Google Scholar 

  62. Verpoorte, J. A., and F. M. Smith. 1972. The optical activity, scattering and viscosity of erythrocyte membranes. Can. J. Biochem. 50: 177–185.

    CAS  Google Scholar 

  63. Juliano, R. L. 1973. The proteins of the erythrocyte membrane. Biochim. Biophys. Acta 300: 341–378.

    PubMed  CAS  Google Scholar 

  64. Green, J. R., P. A. Edwards, and C. Green. 1973. Optical-rotatory dispersion studies of compounds related to cholesterol in liposomes and the membranes of erythrocyte “ghosts.” Biochem. J. 135: 6371–6380.

    Google Scholar 

  65. Luer, C. A., and K.-P. Wong. 1978. The effects of pH and temperature on the CD of human erythrocyte membranes. Biophys. Chem. 9: 15–22.

    PubMed  CAS  Google Scholar 

  66. Maestre, M. F., and J. E. Katz. 1982. A circular dichroism microspectrophotometer. Biopolymers 21: 1899–1908.

    CAS  Google Scholar 

  67. Lenaz, G., and G. Curatola. 1975. Perturbation of membrane fluidity. J. Bioenerg. 7: 223–299.

    CAS  Google Scholar 

  68. Sjoholm, I., and B. Ekman. 1975. Scattering of light—A serious potential risk in CD measurements in the far UV region. Anal. Biochem. 65: 596–599.

    PubMed  CAS  Google Scholar 

  69. Wu, C.-S. C., A. Hachimori, and J. T. Yang. 1982. Lipid-in- duced ordered conformation of some peptide hormones and bioac- tive oligopeptides: Predominance of helix over β form. Biochemistry 21: 4556 - 4562.

    PubMed  CAS  Google Scholar 

  70. Becher, B., and J. Y. Cassim. 1976. Effect of light adaptation on the purple membrane structure of Halobacterium halobium. Biophys. J. 16: 1183–1200.

    PubMed  CAS  Google Scholar 

  71. Duysens, L. N. M. 1956. The flattening of the absorption spectrum of suspensions, as compared to that of solutions. Biochim. Biophys. Acta 19: 1–12.

    PubMed  CAS  Google Scholar 

  72. Strom, R., P. Caiafa, and V. Peresempio. 1972. Effect of alkaline pH on the optical properties of native and modified erythrocyte membranes. Biochemistry 11: 1908–1915.

    PubMed  CAS  Google Scholar 

  73. Dorman, B. P., and M. F. Maestre. 1973. Experimental differential light-scattering correction to the circular dichroism of bacteriophage T2. Proc. Natl. Acad. Sci. USA 70: 255–259.

    PubMed  CAS  Google Scholar 

  74. Dea, I. C. M., and D. A. Rees. 1973. Aggregation with change of conformation in solutions of hemicellulose xylans. Carbohydr. Res. 29: 363–372.

    CAS  Google Scholar 

  75. Vogel, D., and J. Rainer. 1974. Conformational changes and proton uptake in the reversible aggregation of tobacco-mosaic- virus protein. Eur. J. Biochem. 41: 607–615.

    PubMed  CAS  Google Scholar 

  76. Homer, R. B., and R. M. Goodman. 1975. Circular dichroism and fluorescence studies on potato virus x and its structural components. Biochim. Biophys. Acta 378: 296–304.

    PubMed  CAS  Google Scholar 

  77. Zeltlmeissl, G., R. Rudolph, and R. Jaenicke. 1979. Reconstitution of lactate dehydrogenase. Noncovalent aggregation versus reactivation. 1. Physical properties and kinetics of aggregation. Biochemistry 18: 5567–5571.

    Google Scholar 

  78. Sugihara, T., E. R. Blout, and B. A. Wallace. 1982. Hydrophobic oligopeptides in solution and in phospholipid vesicles: Synthetic fragments of bacteriorhodopsin. Biochemistry 21: 3444–3450.

    PubMed  CAS  Google Scholar 

  79. Sugihara, T., E. R. Blout, and B. A. Wallace. 1982. Hydrophobic oligopeptides in solution and in phospholipid vesicles: Synthetic fragments of bacteriorhodopsin. Biochemistry 21: 3444–3450.

    PubMed  CAS  Google Scholar 

  80. Litman, B.J. 1972. Effect of light scattering on the circular dichroism of biological membranes. Biochemistry 11: 3243–3247.

    PubMed  CAS  Google Scholar 

  81. Magdalou, J., M. Balland, C. Thirion, and G. Siest. 1979. Effects of membrane perturbation on UDP-glucuronosyl transferase activity in rat liver microsomes: Circular dichroism studies. Chem. Biol. Interact. 27: 255–268.

    PubMed  CAS  Google Scholar 

  82. Holzworth, G., J. Yu, and T. L. Steck. 1976. Heterogeneity in the conformation of different protein fractions from the human erythrocyte membrane. J. Supramol. Struct. Cell. Biochem. 4: 161–168.

    Google Scholar 

  83. Ortner, M. J., M. J. Galvin, C. F. Chignell, and D. I. McRee. 1981. A circular dichroism study of human erythrocyte ghost proteins during exposure to 2450 MHz microwave radiation. Physics 3: 335–347.

    CAS  Google Scholar 

  84. Lüllman, H., S. T. Peters, J. Preuner, andT. Rüther. 1975. Influence of ouabain and dihydroouabain on the circular dichroism of cardiac plasmalemmal microsomes. Naunyn-Schmiedebergs Arch. Pharmacol. 290: 1–19.

    Google Scholar 

  85. Preuner, J. 1976. Circular dichroism of a microsomal plasma membrane fraction from guinea pig ventricular muscle and the influence of ouabain. Naunyn-Schmiedebergs Arch. Pharmacol. 282 (Suppl. 276): R76.

    Google Scholar 

  86. Preuner, J., and T. Rüther. 1982. Influence of decamethonium and suxamethonium on the conformation of tryptophan side chain chromophores of membrane bound extrajunctional acetylcholine receptors. Biochem. Pharmacol. 29: 397–403.

    Google Scholar 

  87. Lenaz, G., and G. Curatola. 1978. Biophysical studies on agents affecting the state of membrane lipids: Biochemical and pharmacological implications. Mol. Cell. Biochem. 22: 3–32.

    PubMed  CAS  Google Scholar 

  88. Oesterhelt, D., and W. Stoeckenius. 1971. Rhodopsinlike protein from the purple membrane of Halobacterium halobium. Nature New Biol. 233: 149–152.

    PubMed  CAS  Google Scholar 

  89. Blaurock, A. E., and W. Stoeckenius. 1971. Structure of the purple membrane. Nature New Biol. 233: 152–154.

    PubMed  CAS  Google Scholar 

  90. Henderson, R., and P. N. Unwin. 1975. Three-dimensional model of purple membrane obtained by electron microscopy. Nature (London) 257: 28–32.

    CAS  Google Scholar 

  91. Unwin, P. N., and R. Henderson. 1975. Molecular structure determination by electron microscopy of unstained crystalline specimens. J. Mol. Biol. 94: 425–440.

    PubMed  CAS  Google Scholar 

  92. Henderson, R. 1975. The structure of the purple membrane from Halobacterium halobium: Analysis of the X-ray diffraction pattern. J. Mol. Biol. 93: 123–138.

    PubMed  CAS  Google Scholar 

  93. Blaurock, A. E. 1975. Bacteriorhodopsin: Transmembrane pump containing a-helix. J. Mol. Biol. 93: 139–158.

    PubMed  CAS  Google Scholar 

  94. Oesterhelt, D., and W. Stoeckenius. 1974. Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane. Methods Enzymol. 31: 667–678.

    PubMed  CAS  Google Scholar 

  95. Krivacic, J. R., D. E. Wisnosky, andD. W. Urry. 1971. A simultaneous absorption and circular dichroism data acquisition system. Anal. Biochem. 43: 547–555.

    PubMed  CAS  Google Scholar 

  96. Urry, D. W. 1974. Corrections for optical rotation data on biomembranes. Methods Enzymol. 32: 220–233.

    PubMed  CAS  Google Scholar 

  97. Mandel, R., and G. D. Fasman. 1974. Thermal denaturation of DNA and DNA.polypeptide complexes: Simultaneous absorption and circular dichroism measurements. Biochem. Biophys. Res. Commun. 59: 672–679.

    PubMed  CAS  Google Scholar 

  98. Meyers, M. B., and N. Swislocki. 1974. Conformational changes in erythrocyte membranes by prostaglandins as measured by circular dichroism. Arch. Biochem. Biophys. 164: 544–550

    PubMed  CAS  Google Scholar 

  99. Braun, V., R. Heinz, J. P. Ohms, and H. Hagenmaier. 1976. Conformational studies on murein-lipoproteins from the outer membranes of Escherichia coli. Eur. J. Biochem. 70: 601–610.

    PubMed  CAS  Google Scholar 

  100. Evdokomov, Y. M., T. L. Pyatigorskaya, V. A. Kadikov, O. F. Polyvtsev, J. Doskocil, J. Koudelka, and Y. M. Varshavsky. 1976. A compact form of double-stranded RNA in solutions containing poly (ethylene glycol). Nucleic Acids Res. 3: 1533–1547.

    Google Scholar 

  101. Lenaz, G., G. Curatola, L. Mazzanti, andE. Bertoli. 1981. Lipid protein interactions in mitochondrial ATPase. Ital. J. Biochem. 30: 290–301.

    PubMed  CAS  Google Scholar 

  102. Rafferty, D. N., J. Y. Cassim, and D. G. McConnell. 1977. CD, ORD and absorption studies on the conformation of bovine rhodopsin in situ and solubilized with detergent. Biophys. Struct. Mech. 2: 277–320.

    CAS  Google Scholar 

  103. Greff, D., F. Torna, S. Fermandjian, M. Low, and L. Kisfaludy. 1976. Conformational studies of corticotropin and constitutive peptides by circular dichroism. Biochim. Biophys. Acta 439: 219–231.

    PubMed  CAS  Google Scholar 

  104. Shinitzky, M., and B. Rivnay. 1977. Degree of exposure of membrane proteins determined by fluorescence quenching. Biochemistry 16: 982–986.

    PubMed  CAS  Google Scholar 

  105. Hollosi, M., and M. Kajtar. 1977. Studies on the conformation of ß-endorphin and its constituent fragments in water and trifluoroethanol by CD spectroscopy. FEBS Lett. 74:185-189.

    PubMed  CAS  Google Scholar 

  106. Dailey, H. A., and P. Strittmatter. 1978. Structural and functional properties of the membrane binding segment of cytochrome b5. J. Biol. Chem. 253: 8203–8209.

    PubMed  CAS  Google Scholar 

  107. Palumbo, M., E. Jaeger, S. Knof, E. Peggion, and E. Wünsch. 1980. Interaction of metal ions with gastrointestinal hormones. FEBS Lett. 119: 158–160.

    PubMed  CAS  Google Scholar 

  108. Jaeger, E., M. Palumbo, E. Peggion, and E. Wünsch. 1981. Correlation between Ca+ + binding, conformation and action of the gastrins. Hepatogastroenterology 28: 64.

    Google Scholar 

  109. Peggion, E., E. Jaeger, S. Knof, L. Moroder, and E. Wuensch. 1981. Conformational aspects of gastrin-related peptides: A circular dichroism study. Biopolymers 20: 633–652.

    PubMed  CAS  Google Scholar 

  110. Lenaz, G. 1974. Lipid-protein interactions in the structure of biological membranes. Sub-Cell. Biochem. 3: 167–248.

    CAS  Google Scholar 

  111. Lin, J.-C., and E. Farber. 1977. Effect of ribosome stripping procedures on antigenicity and conformation of endoplasmic reticulum membrane. Biochem. Biophys. Res. Commun. 76: 1247–1252.

    PubMed  CAS  Google Scholar 

  112. Kimura, H., and M. Futai. 1978. Effects of phospholipids on L- lactate dehydrogenase from membranes of Escherichia coli. J. Biol. Chem. 253: 1095–1100.

    PubMed  CAS  Google Scholar 

  113. Cockle, S. A., R. M. Epaud, J. M. Boggs, andM. A. Moscarello. 1978. Circular dichroism studies on lipid-protein complexes of a hydrophobic myelin protein. Biochemistry 17: 624–629.

    PubMed  CAS  Google Scholar 

  114. Keniry, M. A., and R. Smith. 1979. Circular dichroic analysis of the structure of myelin basic protein and derived peptides bound to detergents and to lipid vesicles. Biochim. Biophys. Acta 578: 381–391.

    PubMed  CAS  Google Scholar 

  115. Lenaz, G., G. Curatola, L. Mazzanti, E. Bertoli, and A. Bigi. 1979. A conformational model for the action of general anesthetics at the membrane level. I. Theoretical considerations. Ital. J. Biochem. 27: 378–400.

    Google Scholar 

  116. Saccomani, G., H. H. Chang, A. Spisni, H. F. Helander, H. L. Spitzer, and G. Sachs. 1979. Effect of phospholipase A2 on purified gastric vesicles. J. Supramol. Struct. Cell. Biochem. 11: 429–444.

    CAS  Google Scholar 

  117. Kendrew, J. C., R. E. Dickerson, B. E. Strandberg, R. G. Hart, D. R. Davies, D. C. Phillips, and V. C. Shore. 1960. Structure of myoglobin: A three-dimensional Fourier synthesis at 2 Á resolution. Nature (London) 185: 422–427.

    CAS  Google Scholar 

  118. Kendrew, J. C., H. C. Watson, B. E. Strandberg, R. E. Dickerson, D. C. Phillips, and V. C. Shore. 1961. A partial determination by X-ray methods, and its correlation with chemical data. Nature (London) 190: 666–670.

    CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Laboratory of Molecular Biophysics, University of Alabama School of Medicine, Birmingham, Alabama, 35294, USA

    Marianna M. Long & Dan W. Urry

Authors
  1. Marianna M. Long
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Dan W. Urry
    View author publications

    You can also search for this author in PubMed Google Scholar

Editor information

Editors and Affiliations

  1. University of Texas Health Science Center at Houston, Houston, Texas, USA

    Thomas E. Andreoli M.D.  & Stanley G. Schultz M.D.  & 

  2. Yale University School of Medicine, New Haven, Connecticut, USA

    Joseph F. Hoffman Ph.D.

  3. University of California, San Diego La Jolla, California, USA

    Darrell D. Fanestil M.D.

Rights and permissions

Reprints and permissions

Copyright information

© 1986 Plenum Publishing Corporation

About this chapter

Cite this chapter

Long, M.M., Urry, D.W. (1986). Absorption and Optical Rotation Spectra of Biological Membranes. In: Andreoli, T.E., Hoffman, J.F., Fanestil, D.D., Schultz, S.G. (eds) Physiology of Membrane Disorders. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-2097-5_6

Download citation

  • DOI: https://doi.org/10.1007/978-1-4613-2097-5_6

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4612-9242-5

  • Online ISBN: 978-1-4613-2097-5

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics

Search

Navigation