作者: Giovanni Colonna , Gaetano Irace , Giuseppe Parlato , Salvatore M. Aloj , Ciro Balestrieri
DOI: 10.1016/0005-2795(78)90590-1
关键词: Peptide 、 Myoglobin 、 Circular dichroism 、 Protein tertiary structure 、 Crystallography 、 Chromophore 、 Stereochemistry 、 Protein structure 、 Imidazole 、 Fluorescence 、 Chemistry 、 Biochemistry, Genetics and Molecular Biology (miscellaneous)
摘要: The perturbing effect of guanidium hydrochloride and pH on the molecular structure water buffalo apomyoglobin has been investigated by circular dichroism in far near ultraviolet fluorescence. In wavelength region between 320 260 nm dichroic spectrum globin is highly structured contributions aromatic chromophores have resolved. Buffalo undergoes a structural transition at neutral which involves elements secondary tertiary structure, as indicated changes activity peptide fluorescence two tryptophanyl residues. possibility charge-transfer complex indole imidazole discussed. A major with abrupt unfolding takes place 5.6 4.3. Below 4.3 helical residues, survive acid transition, appear to be resistent further acidification 2.0 while emission quenched shifted longer wavelengths. occurs also alkali above 10, detected same techniques. relationships sperm whale are