The secondary structure of bacteriorhodopsin in organic solution. A Fourier transform infrared study

Jaume Torres; Esteve Padrós

doi:10.1016/0014-5793(93)81331-S

The secondary structure of bacteriorhodopsin in organic solution. A Fourier transform infrared study

Jaume Torres, Esteve Padrós^*

^*Corresponding author for this work

Facultat de Medicina

Research output: Contribution to journal › Article › peer-review

13 Citations (Scopus)

Abstract

Fourier transform infrared spectroscopy is used to estimate the secondary structure of bacteriorhodopsin dissolved in Chloroform-methanol (1:1 v v), 0.1 M LiClO₄. Curve-fitting of the deconvolved spectra in the amide I region shows that the total content of α-helices, reverse turns and β-sheets are similar to the native state. However, the α_II-helices, which are the major helical class in native bacteriorhodopsin, are greatly decreased in the solubilized sample. Similarly, the reverse turns and the β-sheets are strongly altered.

Original language	English
Pages (from-to)	77-79
Number of pages	3
Journal	FEBS Letters
Volume	318
Issue number	1
DOIs	https://doi.org/10.1016/0014-5793(93)81331-S
Publication status	Published - Feb 22 1993
Externally published	Yes

ASJC Scopus Subject Areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

Keywords

Bacteriorhodopsin
Infrared spectroscopy
Organic solvent
Reverse turn
Secondary structure
α-Helix

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10.1016/0014-5793(93)81331-S

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abstract = "Fourier transform infrared spectroscopy is used to estimate the secondary structure of bacteriorhodopsin dissolved in Chloroform-methanol (1:1 v v), 0.1 M LiClO4. Curve-fitting of the deconvolved spectra in the amide I region shows that the total content of α-helices, reverse turns and β-sheets are similar to the native state. However, the αII-helices, which are the major helical class in native bacteriorhodopsin, are greatly decreased in the solubilized sample. Similarly, the reverse turns and the β-sheets are strongly altered.",

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AU - Torres, Jaume

AU - Padrós, Esteve

PY - 1993/2/22

Y1 - 1993/2/22

N2 - Fourier transform infrared spectroscopy is used to estimate the secondary structure of bacteriorhodopsin dissolved in Chloroform-methanol (1:1 v v), 0.1 M LiClO4. Curve-fitting of the deconvolved spectra in the amide I region shows that the total content of α-helices, reverse turns and β-sheets are similar to the native state. However, the αII-helices, which are the major helical class in native bacteriorhodopsin, are greatly decreased in the solubilized sample. Similarly, the reverse turns and the β-sheets are strongly altered.

AB - Fourier transform infrared spectroscopy is used to estimate the secondary structure of bacteriorhodopsin dissolved in Chloroform-methanol (1:1 v v), 0.1 M LiClO4. Curve-fitting of the deconvolved spectra in the amide I region shows that the total content of α-helices, reverse turns and β-sheets are similar to the native state. However, the αII-helices, which are the major helical class in native bacteriorhodopsin, are greatly decreased in the solubilized sample. Similarly, the reverse turns and the β-sheets are strongly altered.

KW - Bacteriorhodopsin

KW - Infrared spectroscopy

KW - Organic solvent

KW - Reverse turn

KW - Secondary structure

KW - α-Helix

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The secondary structure of bacteriorhodopsin in organic solution. A Fourier transform infrared study

Abstract

ASJC Scopus Subject Areas

Keywords

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