The effect of evolution on homologous proteins

作者: Giovanni Colonna , Gaetano Irace , Giuseppe Parlato , Salvatore M. Aloj , Ciro Balestrieri

DOI: 10.1016/0005-2795(78)90590-1

关键词: PeptideMyoglobinCircular dichroismProtein tertiary structureCrystallographyChromophoreStereochemistryProtein structureImidazoleFluorescenceChemistryBiochemistry, 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

参考文章(51)
Esther Breslow, Frank R.N. Gurd, Reactivity of sperm whale metmyoglobin towards hydrogen ions and p-nitrophenyl acetate. Journal of Biological Chemistry. ,vol. 237, pp. 371- 381 ,(1962) , 10.1016/S0021-9258(18)93929-3
S.C. Harrison, E.R. Blout, REVERSIBLE CONFORMATIONAL CHANGES OF MYOGLOBIN AND APOMYOGLOBIN. Journal of Biological Chemistry. ,vol. 240, pp. 299- 303 ,(1965) , 10.1016/S0021-9258(18)97648-9
D.B. Wetlaufer, Ultraviolet spectra Of Proteins and Amino Acids Advances in Protein Chemistry. ,vol. 17, pp. 303- 390 ,(1963) , 10.1016/S0065-3233(08)60056-X
Harold Edelhoch, Roland E. Lippoldt, The Properties of Bovine Growth Hormone Journal of Biological Chemistry. ,vol. 245, pp. 4199- 4203 ,(1970) , 10.1016/S0021-9258(18)62904-7
Edward P. Kirby, R.F. Steiner, The tryptophan microenvironments in apomyoglobin. Journal of Biological Chemistry. ,vol. 245, pp. 6300- 6306 ,(1970) , 10.1016/S0021-9258(18)62609-2
Esther Breslow, CHANGES IN SIDE CHAIN REACTIVITY ACCOMPANYING THE BINDING OF HEME TO SPERM WHALE APOMYOGLOBIN. Journal of Biological Chemistry. ,vol. 239, pp. 486- 496 ,(1964) , 10.1016/S0021-9258(18)51706-3
E. Hardin Strickland, Meir Wilchek, Joseph Horwitz, Carolyn Billups, Low Temperature Circular Dichroism of Tyrosyl and Tryptophanyl Diketopiperazines Journal of Biological Chemistry. ,vol. 245, pp. 4168- 4177 ,(1970) , 10.1016/S0021-9258(18)62900-X
H Edelhoch, R E Lippoldt, M Wilchek, The Circular Dichroism of Tyrosyl and Tryptophanyl Diketopiperazines Journal of Biological Chemistry. ,vol. 243, pp. 4799- 4805 ,(1968) , 10.1016/S0021-9258(18)93189-3
Esther Breslow, Sherman Beychok, Karl D. Hardman, Frank R.N. Gurd, RELATIVE CONFORMATIONS OF SPERM WHALE METMYOGLOBIN AND APOMYOGLOBIN IN SOLUTION. Journal of Biological Chemistry. ,vol. 240, pp. 304- 309 ,(1965) , 10.1016/S0021-9258(18)97649-0