The secondary structure of bacteriorhodopsin in organic solution. A Fourier transform infrared study.
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 alpha-helices, reverse turns and beta-sheets are similar to the native state. However, the alpha II-helices, which are the major helical class in native bacteriorhodopsin, are greatly decreased in the solubilized sample. Similarly, the reverse turns and the beta-sheets are strongly altered.
Torres
J
J
Departament de Bioquímica i de Biologia Molecular, Facultat de Medicina, Universitat Autònoma de Barcelona, Catalunya, Spain.
Padrós
E
E
D001436:Bacteriorhodopsins / Q000737:chemistry*; D005583:Fourier Analysis; D019617:Halobacterium salinarum; D017433:Protein Structure, Secondary; D012996:Solutions; D013055:Spectrophotometry, Infrared
D012996:Solutions; D001436:Bacteriorhodopsins