Conformational Changes in the Globin Family During Evolution. 1. Analysis of the Evolutionary Role of Insertions and Deletions

Overview

Journal J Mol Evol

Specialty Biochemistry

Date 1984 Jan 1

PMID 6442358

Citations 1

Authors

A A Zharkikh

V V Solovyov

N A Kolchanov

Affiliations

Soon will be listed here.

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 alpha-helices of the globin molecules. Conformational analysis of the packing of the alpha-helices in the spatial structure of globins demonstrated that the fixation of deletions and insertions in the center of an alpha-helix produces a marked distortion of their normal packing. The possible role of deletions and insertions in the evolution of protein families is discussed.

Citing Articles

Single amino acid substitutions producing instability of globular proteins. Calculation of their frequencies in the entire mutational spectra of the alpha- and beta-subunits of human hemoglobin.

Kolchanov N, Shindyalov I J Mol Evol. 1988; 27(2):154-62.

PMID: 3137354 DOI: 10.1007/BF02138376.

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