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. 1996 Jun;70(6):2882–2887. doi: 10.1016/S0006-3495(96)79858-2

Analysis of conformational changes in bacteriorhodopsin upon retinal removal.

J Cladera 1, J Torres 1, E Padrós 1
PMCID: PMC1225268  PMID: 8744326

Abstract

The conformation of bacterioopsin in the apomembrane has been studied by Fourier transform infrared spectroscopy. Resolution enhancement techniques and curve-fitting procedures have been used to determine the secondary structural components from the amide I region. Bacterioopsin contains about 54% helicoidal structure (alpha I and alpha II helices + 3(10) turns), 21% sheets, 16% reverse turns, and 9% unordered structure. Thus, after retinal removal, all of the secondary structural types of bacteriorhodopsin remain present, and only slight quantitative differences appear. On the other hand, H/D exchange studies show that there is a higher degree of exchange for reverse turns and protonated carboxylic lateral chains in bacterioopsin as compared to bacteriorhodopsin. This gives further support to the idea of a more open tertiary structure of bacterioopsin, and to the consideration of the retinal molecule as an important element in complementing the interhelical interactions in bacteriorhodopsin folding.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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