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Comparative and Functional Genomics
Volume 3 (2002), Issue 6, Pages 525-534
Conference review

Flowering Buds of Globular Proteins: Transpiring Simplicity of Protein Organization

1Department of Structural Biology, The Weizmann Institute of Science, PO Box 26, Rehovot 76100, Israel
2Genome Diversity Centre, Institute of Evolution, University of Haifa, Haifa 31905, Israel

Received 31 August 2002; Accepted 14 October 2002

Copyright © 2002 Hindawi Publishing Corporation. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


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.