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Folding, Stability and Shape of Proteins in Crowded Environments: Experimental and Computational Approaches
How the crowded environment inside cells affects folding, stability and structures of proteins is a vital question, since most proteins are made and function inside cells. Here we describe how crowded conditions can be created in vitro and in silico and how we have used this to probe effects on prot...
Autores principales: | , , |
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Formato: | Texto |
Lenguaje: | English |
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Molecular Diversity Preservation International (MDPI)
2009
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2660654/ https://www.ncbi.nlm.nih.gov/pubmed/19333422 http://dx.doi.org/10.3390/ijms10020572 |
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author | Samiotakis, Antonios Wittung-Stafshede, Pernilla Cheung, Margaret S. |
author_facet | Samiotakis, Antonios Wittung-Stafshede, Pernilla Cheung, Margaret S. |
author_sort | Samiotakis, Antonios |
collection | PubMed |
description | How the crowded environment inside cells affects folding, stability and structures of proteins is a vital question, since most proteins are made and function inside cells. Here we describe how crowded conditions can be created in vitro and in silico and how we have used this to probe effects on protein properties. We have found that folded forms of proteins become more compact in the presence of macromolecular crowding agents; if the protein is aspherical, the shape also changes (extent dictated by native-state stability and chemical conditions). It was also discovered that the shape of the macromolecular crowding agent modulates the folding mechanism of a protein; in addition, the extent of asphericity of the protein itself is an important factor in defining its folding speed. |
format | Text |
id | pubmed-2660654 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2009 |
publisher | Molecular Diversity Preservation International (MDPI) |
record_format | MEDLINE/PubMed |
spelling | pubmed-26606542009-03-30 Folding, Stability and Shape of Proteins in Crowded Environments: Experimental and Computational Approaches Samiotakis, Antonios Wittung-Stafshede, Pernilla Cheung, Margaret S. Int J Mol Sci Review How the crowded environment inside cells affects folding, stability and structures of proteins is a vital question, since most proteins are made and function inside cells. Here we describe how crowded conditions can be created in vitro and in silico and how we have used this to probe effects on protein properties. We have found that folded forms of proteins become more compact in the presence of macromolecular crowding agents; if the protein is aspherical, the shape also changes (extent dictated by native-state stability and chemical conditions). It was also discovered that the shape of the macromolecular crowding agent modulates the folding mechanism of a protein; in addition, the extent of asphericity of the protein itself is an important factor in defining its folding speed. Molecular Diversity Preservation International (MDPI) 2009-02-13 /pmc/articles/PMC2660654/ /pubmed/19333422 http://dx.doi.org/10.3390/ijms10020572 Text en © 2009 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland. This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/). |
spellingShingle | Review Samiotakis, Antonios Wittung-Stafshede, Pernilla Cheung, Margaret S. Folding, Stability and Shape of Proteins in Crowded Environments: Experimental and Computational Approaches |
title | Folding, Stability and Shape of Proteins in Crowded Environments: Experimental and Computational Approaches |
title_full | Folding, Stability and Shape of Proteins in Crowded Environments: Experimental and Computational Approaches |
title_fullStr | Folding, Stability and Shape of Proteins in Crowded Environments: Experimental and Computational Approaches |
title_full_unstemmed | Folding, Stability and Shape of Proteins in Crowded Environments: Experimental and Computational Approaches |
title_short | Folding, Stability and Shape of Proteins in Crowded Environments: Experimental and Computational Approaches |
title_sort | folding, stability and shape of proteins in crowded environments: experimental and computational approaches |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2660654/ https://www.ncbi.nlm.nih.gov/pubmed/19333422 http://dx.doi.org/10.3390/ijms10020572 |
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