Abstract
The fundamental concerns in applying optical methods to the study of biomembranes arise from complications introduced by their particulate nature; the basic objective is not solely to describe the actual absorbance by separating it from the effects of light scattering in the heterogeneous system. Moreover, the objective is to correct the spectrum to the absorbance, or difference absorbance, values that would occur if the molecules were uniformly distributed while retaining their membrane conformational state. This, of course, is because the reference state, for which there is much information, is one in which the polypeptide or protein species of interest is molecularly dispersed in solution. In order to proceed in a more sure-footed manner, a brief review of the fundamentals of absorption and the factors that alter absorption inten-sity and spectral position is warranted. Achieving a satisfactory perspective of the fundamentals allows for a more confident approach to the unique problems of membrane systems.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Moscowitz, A. 1960. Theory and analysis of rotatory dispersion curves. In: Optical Rotatory Dispersion. C. Djerassi, ed. McGraw-Hill, New York. pp. 150–177.
la. Urry, D. W. 1970. Spectroscopic Approaches to Biomolecular Conformation. AMA Press, Chicago, Illinois. pp. 33–121.
Kasha, M. 1963. Energy transfer mechanisms and the molecular exciton model for molecular aggregates. Radio. Res. 20: 55–71.
Rhodes, W. 1961. The hypochromism and other spectral properties of helical polynucleotides. J. Am. Chem. Soc. 83: 3609–3617.
Tinoco, Jr., I. 1961. Hypochromism in polynucleotides. J. Am. Chem. Soc. 82:4785–4790; 1961. Optical and other electronic properties of polymers. J. Chem. Phys. 34: 1067.
Urry, D. W. 1973. Determining biomolecular conformations. III. Ultraviolet absorption spectroscopy. Res. Develop. 24: 28–36.
Urry, D. W., et al. 1974. Biochem. Biophys. Res. Commun. 61: 1427–1433.
Urry, D. W. 1972. Protein conformation in biomembranes: Optical rotation and absorption of membrane suspensions. Biochim. Biophys. Acta, Biomembr. Rev. 265: 115–168.
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.
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.
Gordon, D. J., and G. Holzwarth. 1971. Artifacts in the measured optical activity of membrane suspensions. Arch. Biochem. Biophys. 142: 481–488.
Urry, D. W. 1974. Corrections for optical rotation data in biomembranes. In: Methods in Enzymology, Vol. 32. S. P. Colowick and N. O. Kaplan, eds. Academic Press, New York. pp. 220–234.
Oesterhelt, D., and W. Stoeckenius. 1971. Rhodopsin-like protein from the purple membrane of Halobacterium halobium. Nature (New Biol.) 233: 149–152.
Blaurock, A. E., and W. Stoeckenius. 1971. Structure of the purple membrane. Nature (New Biol.) 233: 152–154.
Henderson, R., and P. N. Unwin. 1975. Three-dimensional model of purple membrane obtained by electron microscopy. Nature 257: 28–32.
Unwin, P. N., and R. Henderson. 1975. Molecular structure determination by electron microscopy of unstained crystalline specimens. J. Mol. Biol. 94: 425–440.
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.
Blaurock, A. E. 1975. Bacteriorhodopsin: Transmembrane pump containing a-helix. J. Mol. Biol. 93: 139–158.
Oesterhelt, D., and W. Stoeckenius. 1974. Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane. In: Methods in Enzymology, Vol. 31. S. P. Colowick and N. O. Kaplan, eds. Academic Press, New York. pp. 667–678.
Long, M. M., and D. W. Urry. 1976. Absorption and circular dichroism spectroscopies. In: Membrane Spectroscopy. E. Grell, ed. Springer-Verlag, Berlin and New York.
Quadrifoglio, F., and D. W. Urry. 1968. Ultraviolet rotatory properties of polypeptides in solution. I. Helical poly-L-aianine. J. Am. Chem. Soc. 90: 2755–2760.
Masotti, L., D. W. Urry, and R. Llinas. 1973. Circular dichroism of lobster axonal membranes. Acta Vitami-nol. Enzymol. (Milano) 27: 154–158.
Masotti, L., M. M. Long, G. Sachs, and D. W. Urry. 1972. Circular dichroism of biological membranes. II. Plasma membranes and sarcotubular vesicles. Biochim. Biophys. Acta 266: 7–17.
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.
Urry, D. W., L. Masotti, and J. Krivacic. 1970. Improved ellipticity data for several biological membranes. Biochem. Biophys. Res. Commun. 41:521— 524.
Urry, D. W., and T. H. Ji, 1968. Distortions in circular dichroism patterns of particulate (or membranous) systems. Arch. Biochem. Biophys. 128: 802–807.
Aizono, Y., A. A. Konstantinov, and Y. A. Sharonov. 1974. Effects of growth hormone on ATPase and fluorescence of isolated liver membranes utilizing the fluorescent substrate, 1, N6-etheno-adenosine triphosphate. Arch. Biochem. Biophys. 163: 634–643.
Arutjunjan, A. M. et al. 1974. Magnetic circular dichroism and magnetooptical rotatory dispersion of sub-mitochondrial particles at room and liquid nitrogen temperatures. FEBS Lett. 46: 317–320.
Braun, V. 1975. Covalent lipoprotein from the outer membrane of Escherichia coli. Biochim. Biophys. Acta 415: 325–377.
Brody, M., and B. Nathanson. 1972. Direct and indirect mechanisms of deaggregation by fatty acids in chlorophyll-containing systems. Biophys. J. 12: 774–790.
Dolinger, P. M., M. Kielczewski, J. R. Trudell, G. Barth, R. E. Linden, E. Bunnenberg, and C. Djerassi. 1974. Magnetic circular dichroism studies. XXV. A preliminary investigation of microsomal cytochromes. Proc. Natl. Acad. Sci. U.S.A. 71: 399–403.
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: 63–71.
Grosse, R., J. Malur, and K. R. H. Repke. 1972. Determination of secondary structures in isolated or membrane proteins by computer curve-fitting analysis of infrared and circular dichroic spectra. FEBS Lett. 25: 313–315.
Hardwicke, P. M. D., and N. M. Green. 1974. The effect of delipidation on the adenosine triphosphatase of sarcoplasmic reticulum. Eur. J. Biochem. 42: 183–193.
Ji, T. H. 1973. Circular dichroism of a membrane protein of Neurospora crassa. Biochem. Biophys. Res. Commun. 51: 829–835.
Juliano, R. L. 1973. The proteins of the erythrocyte membrane. Biochem. Biophys. Res. Commun. 300: 341–378.
Khare, R. S. 1975. X-ray, electron and optical studies on membrane-drug interactions. Stud. Biophys. 48: 161–172.
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.
Laggner, P. 1975. A highly «-helical structure protein in sarcoplasmic reticulum membranes. Nature 255: 427–428.
Litman, B. J. 1972. Effect of light scattering on the circular dichroism of biological membranes. Biochemistry 11: 3243–3247.
Lüllman, H., T. Peters, J. Preuner, and T. Rüther. 1975. Influence of ouabain and dihydroouabain on the circular dichroism of cardiac plasmalemmal microsomes. Naunyn Schmiedebergs Arch. Pharmcol. 290: 1–19.
Moore, W. V., and D. B. Wetlaufer. 1973. Circular dichroism of nerve membrane fractions: Effects of temperature, pH and electrolytes. J. Neurochem. 20: 135–149.
Rottem, S., and L. Hayflick. 1973. Circular dichroism analysis of native and reaggregated mycoplasma membranes. Can. J. Biochem. 51: 632–636.
Rubin, M. S., N. I. Swislock, and M. Sonenberg. 1973. Alteration of liver plasma membrane protein conformation by bovine growth hormone in vitro. Arch. Biochem. Biophys. 157: 252–259.
Singer, J. A., and M. Morrison. 1972. Circular dichroism of human erythrocyte membranes solubilized by iV-pentanol. Biochim. Biophys. Acta 274: 64–70.
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.
Strom, R., P. Caiafa, and B. Mondovi. 1972. Effect of alkaline pH on the optical properties of native and modified erythrocyte membranes. Biochemistry 11: 1908–1915.
Verpoorte, J. A., and F. M. Smith. 1972. The optical activity, scattering, and viscosity of erythrocyte membranes. Can. J. Biochem. 50: 177–185.
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.
Khare, R. S., R. K. Mishra, W. H. Falor, and A. J. Hopfinger. 1974. The circular dichroism of sphingomyelin. Curr. Sci. 43: 67–71.
Litman, B. J., and Y. Barenholz. 1975. The optical activity of D-erythro-sphingomyelin and its contribution to the circular dichroism of sphingomyelin systems. Biochim. Biophys. Acta 394: 166–172.
Yu, K., J. J. Baldessare, and C. Ho. 1974. Physical-chemical studies of phospholipids and poly(amino acids) interactions. Biochemistry 13: 4375–4381.
Dea, I. C. M., and D. A. Rees. 1973. Aggregation with change of conformation in solutions of hemicellulose xylans. Carbohydr. Res. 29: 363–372.
Gelman, R. A., and J. Blackwell. 1973. Interactions between mucopolysaccharides and cationic polypeptides in aqueous solution: Chondroitin 4-sulfate and dermatan sulfate. Biopolymers 12: 1959–1974.
Gelman, R. A., and J. Blackwell. 1973. Heparin-polypeptide interactions in aqueous solution. Arch. Biochem. Biophys. 159: 427–433.
Schodt, K. P., and J. Blackwell. 1976. Comparison of 4-proteoglycans in terms of their interactions with poly(L-arginine). Biopolymers 15: 469–482.
Burnotte, J., B. D. Stollar, and G. D. Fasman. 1973. Immunological and circular dichroism studies of mal-eylated f-1 (A) histone and complexes with DNA. Arch. Biochem. Biophys. 155: 428–435.
Day, L. A. 1973. Circular dichroism and ultraviolet absorption of a deoxyribonucleic acid binding protein of filamentous bacteriophage. Biochemistry 12: 5329–5339.
Spelsberg, T. C., W. M. Mitchell, and F. Chytil. 1973. Structural alterations of acidic proteins by acid treatment of chromatin. Mol. Cell. Biochem. 1: 243–246.
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.
Dorman, B. P., and M. F. Maestre. 1973. Experimental differential light-scattering correction to the circular dichroism of bacteriophage T2. Proc. Natl. Acad. Sci. U.S.A. 70: 255–259.
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.
Rosenheck, K., and A. S. Schneider. 1973. Circular dichroism of chromaffin granule proteins in situ: Analysis of turbidity effects and protein conformation. Proc. Natl.. Acad. Sci. U.S.A. 70: 3458–3462.
Schooley, R. E., and Govindjee. 1976. Cation-induced changes in the circular dichroism spectrum of chloro-plasts. FEBS Lett. 65: 123–125.
Barron, L. D., and A. D. Buckingham. 1975. Rayleigh and Raman optical activity. Annu. Rev. Phys. Chem. 26: 381–396.
Bohren, C. F. 1974. Light scattering by an optically active sphere. Chem. Phys. Lett. 29: 458–462.
Sjoholm, I., and B. Ekman. 1975. Scattering of light— A serious potential risk in circular dichroism measurements in the far ultraviolet region. Anal. Biochem. 65: 596–599.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1980 Springer Science+Business Media New York
About this chapter
Cite this chapter
Urry, D.W., Long, M.M. (1980). Ultraviolet Absorption, Circular Dichroism, and Optical Rotatory Dispersion in Biomembrane Studies. In: Andreoli, T.E., Hoffman, J.F., Fanestil, D.D. (eds) Membrane Physiology. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-1718-1_6
Download citation
DOI: https://doi.org/10.1007/978-1-4757-1718-1_6
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4757-1720-4
Online ISBN: 978-1-4757-1718-1
eBook Packages: Springer Book Archive