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New technologies to analyse protein function: an intrinsic disorder perspective
Functions of intrinsically disordered proteins do not require structure. Such structure-independent functionality has melted away the classic rigid “lock and key” representation of structure–function relationships in proteins, opening a new page in protein science, where molten keys operate on melte...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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F1000 Research Limited
2020
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7014577/ https://www.ncbi.nlm.nih.gov/pubmed/32089835 http://dx.doi.org/10.12688/f1000research.20867.1 |
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author | Uversky, Vladimir N. |
author_facet | Uversky, Vladimir N. |
author_sort | Uversky, Vladimir N. |
collection | PubMed |
description | Functions of intrinsically disordered proteins do not require structure. Such structure-independent functionality has melted away the classic rigid “lock and key” representation of structure–function relationships in proteins, opening a new page in protein science, where molten keys operate on melted locks and where conformational flexibility and intrinsic disorder, structural plasticity and extreme malleability, multifunctionality and binding promiscuity represent a new-fangled reality. Analysis and understanding of this new reality require novel tools, and some of the techniques elaborated for the examination of intrinsically disordered protein functions are outlined in this review. |
format | Online Article Text |
id | pubmed-7014577 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | F1000 Research Limited |
record_format | MEDLINE/PubMed |
spelling | pubmed-70145772020-02-20 New technologies to analyse protein function: an intrinsic disorder perspective Uversky, Vladimir N. F1000Res Review Functions of intrinsically disordered proteins do not require structure. Such structure-independent functionality has melted away the classic rigid “lock and key” representation of structure–function relationships in proteins, opening a new page in protein science, where molten keys operate on melted locks and where conformational flexibility and intrinsic disorder, structural plasticity and extreme malleability, multifunctionality and binding promiscuity represent a new-fangled reality. Analysis and understanding of this new reality require novel tools, and some of the techniques elaborated for the examination of intrinsically disordered protein functions are outlined in this review. F1000 Research Limited 2020-02-10 /pmc/articles/PMC7014577/ /pubmed/32089835 http://dx.doi.org/10.12688/f1000research.20867.1 Text en Copyright: © 2020 Uversky VN http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Review Uversky, Vladimir N. New technologies to analyse protein function: an intrinsic disorder perspective |
title | New technologies to analyse protein function: an intrinsic disorder perspective |
title_full | New technologies to analyse protein function: an intrinsic disorder perspective |
title_fullStr | New technologies to analyse protein function: an intrinsic disorder perspective |
title_full_unstemmed | New technologies to analyse protein function: an intrinsic disorder perspective |
title_short | New technologies to analyse protein function: an intrinsic disorder perspective |
title_sort | new technologies to analyse protein function: an intrinsic disorder perspective |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7014577/ https://www.ncbi.nlm.nih.gov/pubmed/32089835 http://dx.doi.org/10.12688/f1000research.20867.1 |
work_keys_str_mv | AT uverskyvladimirn newtechnologiestoanalyseproteinfunctionanintrinsicdisorderperspective |