Conformational changes in the globin family during evolution

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Abstract
Conformational restrictions imposed on the fixation of insertions and deletions by the three-dimensional structure of globins during evolution are analyzed. An evolutionary tree for the primary structure of 38 taxonomically distant globins was constructed by a computer method. Based on this tree, the calculated fixation frequency of point mutations was 50-fold higher than that established jointly for deletions and insertions, and the fixation frequency of deletions was more than three times that established for insertions. It was also found that deletions and insertions are predominantly fixed in the interhelical sections and at the ends of the α-helices of the globin molecules. Conformational analysis of the packing of the α-helices in the spatial structure of globins demonstrated that the fixation of deletions and insertions in the center of an α-helix produces a marked distortion of their normal packing. The possible role of deletions and insertions in the evolution of protein families is discussed.