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Flowering Buds of Globular Proteins: Transpiring Simplicity of Protein Organization

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Author(s): Igor N. Berezovsky | Edward N. Trifonov

Journal: Comparative and functional genomics.
ISSN 1531-6912

Volume: 3;
Issue: 6;
Start page: 525;
Date: 2006;
Original page

ABSTRACT
Structural and functional complexity of proteins is dramatically reduced to a simple linear picture when the laws of polymer physics are considered. A basic unit of the protein structure is a nearly standard closed loop of 25–35 amino acid residues, and every globular protein is built of consecutively connected closed loops. The physical necessity of the closed loops had been apparently imposed on the early stages of protein evolution. Indeed, the most frequent prototype sequence motifs in prokaryotic proteins have the same sequence size, and their high match representatives are found as closed loops in crystallized proteins. Thus, the linear organization of the closed loop elements is a quintessence of protein evolution, structure and folding.
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