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The alphabet of intrinsic disorder: I. Act like a Pro: On the abundance and roles of proline residues in intrinsically disordered proteins
A significant fraction of every proteome is occupied by biologically active proteins that do not form unique three-dimensional structures. These intrinsically disordered proteins (IDPs) and IDP regions (IDPRs) have essential biological functions and are characterized by extensive structural plastici...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Taylor & Francis
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5424786/ https://www.ncbi.nlm.nih.gov/pubmed/28516008 http://dx.doi.org/10.4161/idp.24360 |
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author | Theillet, Francois-Xavier Kalmar, Lajos Tompa, Peter Han, Kyou-Hoon Selenko, Philipp Dunker, A. Keith Daughdrill, Gary W. Uversky, Vladimir N |
author_facet | Theillet, Francois-Xavier Kalmar, Lajos Tompa, Peter Han, Kyou-Hoon Selenko, Philipp Dunker, A. Keith Daughdrill, Gary W. Uversky, Vladimir N |
author_sort | Theillet, Francois-Xavier |
collection | PubMed |
description | A significant fraction of every proteome is occupied by biologically active proteins that do not form unique three-dimensional structures. These intrinsically disordered proteins (IDPs) and IDP regions (IDPRs) have essential biological functions and are characterized by extensive structural plasticity. Such structural and functional behavior is encoded in the amino acid sequences of IDPs/IDPRs, which are enriched in disorder-promoting residues and depleted in order-promoting residues. In fact, amino acid residues can be arranged according to their disorder-promoting tendency to form an alphabet of intrinsic disorder that defines the structural complexity and diversity of IDPs/IDPRs. This review is the first in a series of publications dedicated to the roles that different amino acid residues play in defining the phenomenon of protein intrinsic disorder. We start with proline because data suggests that of the 20 common amino acid residues, this one is the most disorder-promoting. |
format | Online Article Text |
id | pubmed-5424786 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Taylor & Francis |
record_format | MEDLINE/PubMed |
spelling | pubmed-54247862017-05-17 The alphabet of intrinsic disorder: I. Act like a Pro: On the abundance and roles of proline residues in intrinsically disordered proteins Theillet, Francois-Xavier Kalmar, Lajos Tompa, Peter Han, Kyou-Hoon Selenko, Philipp Dunker, A. Keith Daughdrill, Gary W. Uversky, Vladimir N Intrinsically Disord Proteins Review A significant fraction of every proteome is occupied by biologically active proteins that do not form unique three-dimensional structures. These intrinsically disordered proteins (IDPs) and IDP regions (IDPRs) have essential biological functions and are characterized by extensive structural plasticity. Such structural and functional behavior is encoded in the amino acid sequences of IDPs/IDPRs, which are enriched in disorder-promoting residues and depleted in order-promoting residues. In fact, amino acid residues can be arranged according to their disorder-promoting tendency to form an alphabet of intrinsic disorder that defines the structural complexity and diversity of IDPs/IDPRs. This review is the first in a series of publications dedicated to the roles that different amino acid residues play in defining the phenomenon of protein intrinsic disorder. We start with proline because data suggests that of the 20 common amino acid residues, this one is the most disorder-promoting. Taylor & Francis 2013-04-01 /pmc/articles/PMC5424786/ /pubmed/28516008 http://dx.doi.org/10.4161/idp.24360 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 | Review Theillet, Francois-Xavier Kalmar, Lajos Tompa, Peter Han, Kyou-Hoon Selenko, Philipp Dunker, A. Keith Daughdrill, Gary W. Uversky, Vladimir N The alphabet of intrinsic disorder: I. Act like a Pro: On the abundance and roles of proline residues in intrinsically disordered proteins |
title | The alphabet of intrinsic disorder: I. Act like a Pro: On the abundance and roles of proline residues in intrinsically disordered proteins |
title_full | The alphabet of intrinsic disorder: I. Act like a Pro: On the abundance and roles of proline residues in intrinsically disordered proteins |
title_fullStr | The alphabet of intrinsic disorder: I. Act like a Pro: On the abundance and roles of proline residues in intrinsically disordered proteins |
title_full_unstemmed | The alphabet of intrinsic disorder: I. Act like a Pro: On the abundance and roles of proline residues in intrinsically disordered proteins |
title_short | The alphabet of intrinsic disorder: I. Act like a Pro: On the abundance and roles of proline residues in intrinsically disordered proteins |
title_sort | alphabet of intrinsic disorder: i. act like a pro: on the abundance and roles of proline residues in intrinsically disordered proteins |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5424786/ https://www.ncbi.nlm.nih.gov/pubmed/28516008 http://dx.doi.org/10.4161/idp.24360 |
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