Home LiteratureArticle Details
PMID: 262400 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Polarized infrared spectroscopy of oriented purple membrane.

Biophysical journal ·Vol. 25 ·No. 3 ·1979-03-00 ·Pages 473-87

Rothschild KJ, Clark NA

Abstract

Polarized Fourier transform infrared spectroscopy has been used to study the structure of purple membrane from Halobacterium halobium. Membranes were oriented by drying a suspension of membrane fragments onto Irtran-4 slides. Dichroism measurements of the amide I, II and A peaks were used to find the average spatial orientation of the bacteriorhodopsin alpha-helices. By deriving a function that relates the observed dichroism to the orientational order parameters for the peptide groups, helical axis distribution, and mosaic spread of the membranes, the average orientation of the alpha-helices was found to lie in a range of less than 26 degrees away from the membrane normal, agreeing with electron microscopic measurements. The frequency of the amide I and A peaks is at least 10 cm-1 higher than values found for most alpha-helical polypeptides and proteins. This may indicate that bacteriorhodopsin contains distorted alpha-helical conformations.

MeSH Terms
Bacteriorhodopsins Carotenoids Circular Dichroism Fourier Analysis Halobacterium/analysis Mathematics Models, Biological Protein Conformation Spectrophotometry, Infrared
Chemicals
Carotenoids Bacteriorhodopsins
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Rothschild K J
Clark N A
References (22)
22 references, click to expand
  1. Infrared spectra and chain conformation of proteins.
    J Mol Biol. 1962 Jun;4:528-40 PMID: 14459672
  2. Transient and linear dichroism studies on bacteriorhodopsin: determination of the orientation of the 568 nm all-trans retinal chromophore.
    J Mol Biol. 1977 Dec 15;117(3):607-20 PMID: 609098
  3. Stereochemical considerations for constructing alpha-helical protein bundles with particular application to membrane proteins.
    Biochem J. 1977 Apr 1;163(1):45-57 PMID: 869919
  4. Kinetic resonance Raman spectroscopy: dynamics of deprotonation of the Schiff base of bacteriorhodopsin.
    Science. 1977 Mar 25;195(4284):1328-30 PMID: 841330
  5. Effects of light adaptation on the purple membrane structure of Halobacterium halobium.
    Biophys J. 1976 Oct;16(10):1183-200 PMID: 963198
  6. Structure of the purple membrane.
    Nat New Biol. 1971 Sep 29;233(39):152-5 PMID: 5286750
  7. Opsin structure probed by raman spectroscopy of photoreceptor membranes.
    Science. 1976 Mar 19;191(4232):1176-8 PMID: 1257742
  8. The structure of the purple membrane from Halobacterium hallobium: analysis of the X-ray diffraction pattern.
    J Mol Biol. 1975 Apr 5;93(2):123-38 PMID: 239244
  9. Light-dependent proton and rubidium translocation in membrane vesicles from Halobacterium halobium.
    Biochem Biophys Res Commun. 1975 Jan 2;64(3):1054-61 PMID: 238520
  10. Functions of a new photoreceptor membrane.
    Proc Natl Acad Sci U S A. 1973 Oct;70(10):2853-7 PMID: 4517939
  11. Tunable laser resonance raman spectroscopy of bacteriorhodopsin.
    Proc Natl Acad Sci U S A. 1974 Nov;71(11):4462-6 PMID: 4530995
  12. Light energy conversion in Halobacterium halobium.
    J Supramol Struct. 1974;2(5-6):769-74 PMID: 4461852
  13. Conformational analysis of phosphatidylethanol-amine in multilayers by infrared dichroism.
    Chem Phys Lipids. 1975 Nov;15(2):222-42 PMID: 1204133
  14. Bacteriorhodospin: a trans-membrane pump containing alpha-helix.
    J Mol Biol. 1975 Apr 5;93(2):139-58 PMID: 1152049
  15. AlphaDL and piDL helices of alternating poly-gamma-benzyl-D-L-glutamate.
    J Mol Biol. 1975 Feb 15;92(1):1-13 PMID: 1152039
  16. Three-dimensional model of purple membrane obtained by electron microscopy.
    Nature. 1975 Sep 4;257(5521):28-32 PMID: 1161000
  17. Improved isolation procedures for the purple membrane of Halobacterium halobium.
    Prep Biochem. 1975;5(2):161-78 PMID: 1144313
  18. Characterization and composition of the purple and red membrane from Halobacterium cutirubrum;.
    Can J Biochem. 1975 Mar;53(3):284-92 PMID: 1125815
  19. Infrared spectra of plasma membrane and endoplasmic reticulum of Ehrlich ascites carcinoma.
    Biochim Biophys Acta. 1968 Mar 1;150(2):186-93 PMID: 5689246
  20. Infrared spectra and the chain organization of erythrocyte membranes.
    Science. 1968 Apr 19;160(3825):314-6 PMID: 5641262
  21. Infrared spectra and protein conformations in aqueous solutions. II. Survey of globular proteins.
    J Biol Chem. 1967 Dec 10;242(23):5467-73 PMID: 12325361
  22. Infrared spectra and protein conformations in aqueous solutions. I. The amide I band in H2O and D2O solutions.
    J Biol Chem. 1967 Dec 10;242(23):5460-6 PMID: 12325360
Article Info
Journal
Biophysical journal
Abbr.
Biophys J
ISSN
0006-3495
DOI
10.1016/S0006-3495(79)85317-5
Published
1979-03-00
Pages
473-87
Language
English
Region
United States
NLM ID
0370626
PMCID
PMC1328485
Subset
IM
External Links
PubMed source DOI: 10.1016/S0006-3495(79)85317-5 PMC Full Text View journal details
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: [email protected]

Copyright © 2026.Genelibs Jinan Honghui Biotechnology Co., Ltd. 鲁ICP备20007159号-2