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Hemoglobin folding pattern

Figure 7-23 Folding pattern of the hemoglobin monomers. The pattern shown is for the P chain of human hemoglobin. Some of the differences between this and the a chain and myoglobin are indicated. Evolutionarily conserved residues are indicated by boxes, I I highly conserved, I I invariant. Other markings show substitutions observed in some abnormal human hemoglobins. Conserved residues are numbered according to their location in one of the helices A-H, while mutant hemoglobins are indicated by the position of the substitution in the entire a and P chain. Figure 7-23 Folding pattern of the hemoglobin monomers. The pattern shown is for the P chain of human hemoglobin. Some of the differences between this and the a chain and myoglobin are indicated. Evolutionarily conserved residues are indicated by boxes, I I highly conserved, I I invariant. Other markings show substitutions observed in some abnormal human hemoglobins. Conserved residues are numbered according to their location in one of the helices A-H, while mutant hemoglobins are indicated by the position of the substitution in the entire a and P chain.

See other pages where Hemoglobin folding pattern is mentioned: [Pg.352]    [Pg.362]    [Pg.352]    [Pg.362]    [Pg.75]    [Pg.268]    [Pg.99]    [Pg.407]    [Pg.353]    [Pg.353]    [Pg.82]    [Pg.244]    [Pg.65]    [Pg.89]    [Pg.353]    [Pg.353]    [Pg.135]    [Pg.232]    [Pg.117]    [Pg.40]   
See also in sourсe #XX -- [ Pg.354 ]

See also in sourсe #XX -- [ Pg.354 ]

See also in sourсe #XX -- [ Pg.354 ]

See also in sourсe #XX -- [ Pg.354 ]




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