Literature DB >> 19431673

Electrodichroism of purple membrane: ionic strength dependence.

E Papp, G Fricsovszky, G Meszéna.   

Abstract

The dichroism of purple membrane suspension was measured in dc and ac electric fields. From these measurements three parameters can be obtained: the permanent dipole moment, mu, the electrical polarizability, alpha, and the retinal angle, delta, (relative to the membrane normal). The functional dependence of the dichroism on the electric field is analyzed. There is a small decrease ( approximately 2 degrees ) in retinal angle going from dark adapted to the light adapted form. No measurable difference in mu, alpha, and delta was found under the photocycle. The dichroism was measured in two different salt solutions (KCl and CaCl(2)) in the range 0-10 mM. The retinal angle increases from 64 degrees to 68 degrees with increasing ionic strength going through a minimum. This is attributed to the changing (decreasing) inner electric field in the membrane. The polarizability, alpha, consists of two parts. One component is related to the polarization of the purple membrane and the second component to the ionic cloud. The second component decreases with ion concentration approximately as kappa(-3) (kappa is the Debye parameter) in agreement with a model calculation for the polarization of the ionic cloud. The origin of the slightly ionic strength dependent permanent dipole moment is not well understood.

Entities:  

Year:  1986        PMID: 19431673      PMCID: PMC1329689          DOI: 10.1016/S0006-3495(86)83737-7

Source DB:  PubMed          Journal:  Biophys J        ISSN: 0006-3495            Impact factor:   4.033


  11 in total

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Authors:  R Shinar; S Druckmann; M Ottolenghi; R Korenstein
Journal:  Biophys J       Date:  1977-07       Impact factor: 4.033

2.  Anisotropic electric properties of purple membrane and their change during the photoreaction cycle.

Authors:  Y Kimura; M Fujiwara; A Ikegami
Journal:  Biophys J       Date:  1984-03       Impact factor: 4.033

3.  Light activates rotations of bacteriorhodopsin in the purple membrane.

Authors:  P L Ahl; R A Cone
Journal:  Biophys J       Date:  1984-06       Impact factor: 4.033

4.  Electric dichroism in the purple membrane of Halobacterium halobium.

Authors:  S Druckmann; M Ottolenghi
Journal:  Biophys J       Date:  1981-02       Impact factor: 4.033

5.  Peptide-chain secondary structure of bacteriorhodopsin.

Authors:  B K Jap; M F Maestre; S B Hayward; R M Glaeser
Journal:  Biophys J       Date:  1983-07       Impact factor: 4.033

6.  Electro-optical measurements on aqueous suspension of purple membrane from Halobacterium halobium.

Authors:  K Barabás; A Dér; Z Dancsházy; P Ormos; L Keszthelyi; M Marden
Journal:  Biophys J       Date:  1983-07       Impact factor: 4.033

7.  Dipoles of the alpha-helix and beta-sheet: their role in protein folding.

Authors:  W G Hol; L M Halie; C Sander
Journal:  Nature       Date:  1981-12-10       Impact factor: 49.962

8.  Orientation of membrane fragments by electric field.

Authors:  L Keszthelyi
Journal:  Biochim Biophys Acta       Date:  1980-06-06

9.  Interfacial electric polarizability of purple membranes in solution.

Authors:  G Todorov; S Sokerov; S P Stoylov
Journal:  Biophys J       Date:  1982-10       Impact factor: 4.033

10.  Bacteriorhodopsin is an inside-out protein.

Authors:  D M Engelman; G Zaccai
Journal:  Proc Natl Acad Sci U S A       Date:  1980-10       Impact factor: 11.205

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  4 in total

1.  Effect of membrane potential on the conformation of bacteriorhodopsin reconstituted in lipid vesicles.

Authors:  V Brumfeld; I R Miller
Journal:  Biophys J       Date:  1988-10       Impact factor: 4.033

2.  Measuring local surface charge densities in electrolyte solutions with a scanning force microscope.

Authors:  H J Butt
Journal:  Biophys J       Date:  1992-08       Impact factor: 4.033

3.  Electrostatics and electrodynamics of bacteriorhodopsin.

Authors:  D Porschke
Journal:  Biophys J       Date:  1996-12       Impact factor: 4.033

4.  Long- and short-range electrostatic interactions affect the rheology of highly concentrated antibody solutions.

Authors:  Ravi Chari; Kavita Jerath; Advait V Badkar; Devendra S Kalonia
Journal:  Pharm Res       Date:  2009-10-01       Impact factor: 4.200

  4 in total

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