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Flowering Buds of Globular Proteins: Transpiring Simplicity of Protein Organization

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 consecutive...

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Detalles Bibliográficos
Autores principales: Berezovsky, Igor N., Trifonov, Edward N.
Formato: Texto
Lenguaje:English
Publicado: Hindawi Publishing Corporation 2002
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2448413/
https://www.ncbi.nlm.nih.gov/pubmed/18629251
http://dx.doi.org/10.1002/cfg.223
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author Berezovsky, Igor N.
Trifonov, Edward N.
author_facet Berezovsky, Igor N.
Trifonov, Edward N.
author_sort Berezovsky, Igor N.
collection PubMed
description 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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spelling pubmed-24484132008-07-14 Flowering Buds of Globular Proteins: Transpiring Simplicity of Protein Organization Berezovsky, Igor N. Trifonov, Edward N. Comp Funct Genomics Research Article 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. Hindawi Publishing Corporation 2002-12 /pmc/articles/PMC2448413/ /pubmed/18629251 http://dx.doi.org/10.1002/cfg.223 Text en Copyright © 2002 Hindawi Publishing Corporation. http://creativecommons.org/licenses/by/ 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.
spellingShingle Research Article
Berezovsky, Igor N.
Trifonov, Edward N.
Flowering Buds of Globular Proteins: Transpiring Simplicity of Protein Organization
title Flowering Buds of Globular Proteins: Transpiring Simplicity of Protein Organization
title_full Flowering Buds of Globular Proteins: Transpiring Simplicity of Protein Organization
title_fullStr Flowering Buds of Globular Proteins: Transpiring Simplicity of Protein Organization
title_full_unstemmed Flowering Buds of Globular Proteins: Transpiring Simplicity of Protein Organization
title_short Flowering Buds of Globular Proteins: Transpiring Simplicity of Protein Organization
title_sort flowering buds of globular proteins: transpiring simplicity of protein organization
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2448413/
https://www.ncbi.nlm.nih.gov/pubmed/18629251
http://dx.doi.org/10.1002/cfg.223
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