The secondary structure of bacteriorhodopsin in organic solution
- 22 February 1993
- journal article
- Published by Wiley in FEBS Letters
- Vol. 318 (1) , 77-79
- https://doi.org/10.1016/0014-5793(93)81331-s
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.Keywords
This publication has 19 references indexed in Scilit:
- New insight into protein secondary structure from resolution-enhanced infrared spectraPublished by Elsevier ,2003
- Three‐dimensional structure of (1–36)bacterioopsin in methanol—chloroform mixture and SDS micelles determined by 2D 1H‐NMR spectroscopyFEBS Letters, 1992
- Three‐dimensional structure of proteolytic fragment 163–231 of bacterioopsin determined from nuclear magnetic resonance data in solutionEuropean Journal of Biochemistry, 1992
- Sequence‐specific 1H‐NMR assignment and conformation of proteolytic fragment 163–231 of bacterioopsinEuropean Journal of Biochemistry, 1990
- Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopyJournal of Molecular Biology, 1990
- Membrane protein folding and oligomerization: the two-stage modelBiochemistry, 1990
- Protein secondary structures in water from second-derivative amide I infrared spectraBiochemistry, 1990
- Mobility and solvent exposure of aromatic residues in bacteriorhodopsin investigated by 1H‐NMR and photo‐CIDNP‐NMR spectroscopyFEBS Letters, 1988
- 19F NMR study of 5‐fluorotryptophan‐labeled bacteriorhodopsinFEBS Letters, 1987
- Rhodopsin and bacteriorhodopsin: structure—function relationshipsFEBS Letters, 1982