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Hemoglobin comparison with myoglobin

A comparison of the two chains of hemoglobin with myoglobin was made by Watson and Kendrew (1961), Braunitzer et al. (1961a, b), Keil and Sorm (1962), and Sorm (1962a, b). Structural relations between cytochrome c and the remaining heme proteins were studied by Sorm (1962c). [Pg.194]

Figure 7.5. Comparing the Amino Acid Sequences of Hemoglobin a and myoglobin. (A) A comparison is made by sliding the sequences of the two proteins past one another, one amino acid at a time, and counting the number of amino acid identities between the proteins. (B) The two alignments with the largest number of matches are shown above the graph, which plots the matches as a function of alignment. Figure 7.5. Comparing the Amino Acid Sequences of Hemoglobin a and myoglobin. (A) A comparison is made by sliding the sequences of the two proteins past one another, one amino acid at a time, and counting the number of amino acid identities between the proteins. (B) The two alignments with the largest number of matches are shown above the graph, which plots the matches as a function of alignment.
A classic illustration of the quaternary structure and its effect on protein properties is a comparison of hemoglobin, an allosteric protein, with myoglobin, which consists of a single polypeptide chain. [Pg.106]

Comparison of the pendant imidazole model with myoglobin or isolated hemoglobin chains shows that the model reacts 10 times faster with O2 and that the dissociation rate is approximately 100 times faster than in the natural systems. [Pg.196]

The precise structural identities of the high-valent oxo-iron states of heme systems are also of interest. Recent work by Mayer [101] indicates that the Fe =0 bond of an oxo iron (IV) complex is 0.1 A longer than expected in comparison with other metal oxo complexes. The oxygen-binding respiratory proteins hemoglobin and myoglobin will each form a relatively stable derivative... [Pg.10]

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]

Evolutionary trees can be constructed with the assumption that the number of sequence differences reflects the time since the two sequences diverged. Construction of an evolutionary tree based on sequence comparisons revealed approximate times for the gene-duplication events separating myoglobin and hemoglobin as well as the a and (3 subunits of hemoglobin. Evolutionary trees based on sequences can be compared with those based on fossil records. ... [Pg.180]

The phenomenological observations detailed above in section 7.2.4 clearly exhibit a coherence of phenomena with the consilient mechanism. Our objective, therefore, is to determine the particular expressions of the consilient mechanism at the molecular level. As a starting point, we look from the aqueous medium to the heme group in its protein setting and make gross comparison between the heme environment in myoglobin and the environments of the hemes of hemoglobin. In our view, the first clue... [Pg.265]


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