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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...

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Detalles Bibliográficos
Autores principales: Samiotakis, Antonios, Wittung-Stafshede, Pernilla, Cheung, Margaret S.
Formato: Texto
Lenguaje:English
Publicado: Molecular Diversity Preservation International (MDPI) 2009
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.
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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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