Study of the structure of arrestin (S-antigen) from bovine photoreceptors by FTIR spectroscopy.
Fourier transform-infrared spectroscopy has been used for the study of the secondary structure of arrestin from bovine retina rod cells. Spectra have been obtained in H2O and in D2O media. Resolution enhancement of the amide I secondary structure-sensitive overlapped component bands has been achieved by means of Fourier self-deconvolution and Fourier derivation. In order to obtain a quantitative estimation of the proportion of amino acid residues involved in each type of secondary structure, bands at the resolved frequencies have been curve-fitted to the deconvolved amide I contour by means of a least-squares best-fitting iterative program. The analysis of the results suggests that the secondary structure of arrestin comprises 56-63% of extended strands, 12-19% of turns and bends, 15% of alpha-helices and 10% of undefined and irregular segments.
Garcia-Quintana
D
D
Departament de Bioquímica i de Biologia Molecular, Facultat de Medicina, Universitat Autònoma de Barcelona, Spain.
Garriga
P
P
Manyosa
J
J
D000577:Amides / Q000737:chemistry; D000818:Animals; D000941:Antigens / Q000737:chemistry*; D019393:Arrestin; D002417:Cattle; D003903:Deuterium; D017666:Deuterium Oxide; D005136:Eye Proteins / Q000737:chemistry*; D005583:Fourier Analysis; D010786:Photoreceptor Cells / Q000737:chemistry*; D011487:Protein Conformation; D013055:Spectrophotometry, Infrared / Q000379:methods; D014867:Water
D000577:Amides; D000941:Antigens; D019393:Arrestin; D005136:Eye Proteins; D014867:Water; D003903:Deuterium; D017666:Deuterium Oxide