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Evolution of myoglobin/hemoglobin proteins

See also Evolution of Myoglobin/Hemoglobin Proteins, Hemoglobin Variants, Thalassemias, Generation of Antibody Diversity... [Pg.1872]

See also Hemoglobin Variants, Globin Gene Expression in Development, Evolution of Myoglobin/ Hemoglobin Proteins, Mechanisms of Protein Mutation, Hemoglobin... [Pg.1931]

Evolution of the Myoglobin/Hemoglobin Proteins (Figure 5.14, Figure 7.22, Figure 7.23, Figure... [Pg.2453]

Comparison of the amino acid sequences of hemoglobin and myoglobin chains from different species of animals shows that the chains from related species are similar. The number of differences increases with phylogenetically more separated species. On the assumption that proteins evolve at a constant rate, the number of differences between two homologous proteins will be proportional to the time of divergence in evolution of the species. [Pg.98]

The evolution of cytochrome c and protein molecules in general has been the subject of many papers and reviews, and can be treated relatively briefly here. The starting points must be Anfinson s Molecular Basis of Evolution (57), based on the early amino acid sequence work, and the discovery that same year by Kendrew and Perutz of the identity of three-dimensional folding of the related proteins myoglobin and hemoglobin (98,99). These illustrate the two components of any study of mac-romolecular evolution the chemical sequence of the polymer and the folding of the polymer in three dimensions. [Pg.429]


See other pages where Evolution of myoglobin/hemoglobin proteins is mentioned: [Pg.402]    [Pg.405]    [Pg.1915]    [Pg.1919]    [Pg.1933]    [Pg.402]    [Pg.405]    [Pg.1915]    [Pg.1919]    [Pg.1933]    [Pg.330]    [Pg.168]    [Pg.190]    [Pg.192]    [Pg.183]    [Pg.188]    [Pg.229]    [Pg.498]    [Pg.450]    [Pg.498]    [Pg.1915]    [Pg.1915]    [Pg.1932]    [Pg.348]    [Pg.1142]    [Pg.480]    [Pg.82]    [Pg.13]    [Pg.207]    [Pg.292]   


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