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Lateral domain movements within a protein, which we have designated DOMO (domain movement), represent novel routes for the diversification of proteins.
Our discovery might also shed light on another mysterious issue associated with the diversification of proteins.
Alternative splicing is an important molecular mechanism that significantly contributes to structural and functional diversification of proteins.
Widespread appearance of domain structures in organismal lineages across the three superkingdoms signals massive diversification of proteins and proteomes.
The large structural impact at low energy cost of engineering disulphide bonds represents an opportunity for structural (and functional) diversification of proteins during evolution.
Glycosylation, one of the many types of PTMs, contributes to the diversification of proteins by the addition of structurally-diverse oligosaccharides.
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In the course of evolution, this mechanism has led to major diversification of protein folds and their functionalities.
Qian, Luscombe and Gerstein [J. Molecular Biol. 313 (2001) 673-681] introduced a model of the diversification of protein folds in a genome that we may formulate as follows.
However, diversification of protein function and regulation of expression has evolved via alternate splicing.
However, the evolutionary diversification of protein families often leads to structural differences, which makes their phylogenetic characterization difficult.
DOI: http://dx.doi.org/10.7554/eLife.03526.017 Intrinsic noise results in diversification of protein ratios.
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