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Disorder in the lifetime of a protein

Intrinsic disorder is everywhere and is inevitable. The non-folding propensity is inherent for numerous natural polypeptide chains, and many functional proteins and protein regions are intrinsically disordered. Furthermore, at particular moments in their life, most notably during their synthesis and...

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Detalles Bibliográficos
Autor principal: Uversky, Vladimir N
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Taylor & Francis 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5424783/
https://www.ncbi.nlm.nih.gov/pubmed/28516024
http://dx.doi.org/10.4161/idp.26782
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author Uversky, Vladimir N
author_facet Uversky, Vladimir N
author_sort Uversky, Vladimir N
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description Intrinsic disorder is everywhere and is inevitable. The non-folding propensity is inherent for numerous natural polypeptide chains, and many functional proteins and protein regions are intrinsically disordered. Furthermore, at particular moments in their life, most notably during their synthesis and degradation, all ordered proteins are at least partially unfolded (disordered). Also, there is a widely spread phenomenon of conditional (functional or transient) disorder, where functions of many ordered proteins require local or even global unfolding of their unique structures. Finally, extrinsic disorder (i.e., intrinsic disorder in functional partners of ordered proteins) should be taken into account too. Therefore, even if a protein is completely devoid of intrinsically disordered regions in its mature form (which is a rather exceptional situation), it faces different forms of disorder (intrinsic, extrinsic, or induced disorder) at all the stages of its functional life, from birth to death. The goal of this article is to briefly introduce this concept of disorder in the lifetime of a protein.
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spelling pubmed-54247832017-05-17 Disorder in the lifetime of a protein Uversky, Vladimir N Intrinsically Disord Proteins Perspective Intrinsic disorder is everywhere and is inevitable. The non-folding propensity is inherent for numerous natural polypeptide chains, and many functional proteins and protein regions are intrinsically disordered. Furthermore, at particular moments in their life, most notably during their synthesis and degradation, all ordered proteins are at least partially unfolded (disordered). Also, there is a widely spread phenomenon of conditional (functional or transient) disorder, where functions of many ordered proteins require local or even global unfolding of their unique structures. Finally, extrinsic disorder (i.e., intrinsic disorder in functional partners of ordered proteins) should be taken into account too. Therefore, even if a protein is completely devoid of intrinsically disordered regions in its mature form (which is a rather exceptional situation), it faces different forms of disorder (intrinsic, extrinsic, or induced disorder) at all the stages of its functional life, from birth to death. The goal of this article is to briefly introduce this concept of disorder in the lifetime of a protein. Taylor & Francis 2013-11-07 /pmc/articles/PMC5424783/ /pubmed/28516024 http://dx.doi.org/10.4161/idp.26782 Text en Copyright © 2013 Landes Bioscience http://creativecommons.org/licenses/by-nc/3.0/ This is an open-access article licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported License. The article may be redistributed, reproduced, and reused for non-commercial purposes, provided the original source is properly cited.
spellingShingle Perspective
Uversky, Vladimir N
Disorder in the lifetime of a protein
title Disorder in the lifetime of a protein
title_full Disorder in the lifetime of a protein
title_fullStr Disorder in the lifetime of a protein
title_full_unstemmed Disorder in the lifetime of a protein
title_short Disorder in the lifetime of a protein
title_sort disorder in the lifetime of a protein
topic Perspective
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5424783/
https://www.ncbi.nlm.nih.gov/pubmed/28516024
http://dx.doi.org/10.4161/idp.26782
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