Why Do Tetrapropylammonium Chloride and Sulphate Salts Destabilize the Native State of Globular Proteins?
It has recently been shown that aqueous solutions of tetrapropylammonium chloride and sulphate salts destabilize the folded conformation of Trp-peptides (Dempsey et al., 2011). This result is rationalized by the application of a statistical thermodynamic approach (Graziano, 2010). It is shown that t...
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2014-01-01
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Series: | The Scientific World Journal |
Online Access: | http://dx.doi.org/10.1155/2014/870106 |
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author | Giuseppe Graziano |
author_facet | Giuseppe Graziano |
author_sort | Giuseppe Graziano |
collection | DOAJ |
description | It has recently been shown that aqueous solutions of tetrapropylammonium chloride and sulphate salts destabilize the folded conformation of Trp-peptides (Dempsey et al., 2011). This result is rationalized by the application of a statistical thermodynamic approach (Graziano, 2010). It is shown that the magnitude of the solvent-excluded volume effect, the main contribution for the native state stability, decreases in both aqueous 2 M TPACl solution and aqueous 1 M TPA2SO4 solution. This happens because TPA+ ions are so large in size and interact so weakly with water molecules, due to their very low charge density, to be able to counteract the electrostrictive effect of chloride and sulphate ions on the water structure, so that the density of their aqueous solutions is smaller or only slightly larger than that of water. |
format | Article |
id | doaj-art-f26b5a9827ca4a42b04f532e7fc905b4 |
institution | Kabale University |
issn | 2356-6140 1537-744X |
language | English |
publishDate | 2014-01-01 |
publisher | Wiley |
record_format | Article |
series | The Scientific World Journal |
spelling | doaj-art-f26b5a9827ca4a42b04f532e7fc905b42025-02-03T01:06:42ZengWileyThe Scientific World Journal2356-61401537-744X2014-01-01201410.1155/2014/870106870106Why Do Tetrapropylammonium Chloride and Sulphate Salts Destabilize the Native State of Globular Proteins?Giuseppe Graziano0Dipartimento di Scienze e Tecnologie, Università del Sannio, Via Port’Arsa 11, 82100 Benevento, ItalyIt has recently been shown that aqueous solutions of tetrapropylammonium chloride and sulphate salts destabilize the folded conformation of Trp-peptides (Dempsey et al., 2011). This result is rationalized by the application of a statistical thermodynamic approach (Graziano, 2010). It is shown that the magnitude of the solvent-excluded volume effect, the main contribution for the native state stability, decreases in both aqueous 2 M TPACl solution and aqueous 1 M TPA2SO4 solution. This happens because TPA+ ions are so large in size and interact so weakly with water molecules, due to their very low charge density, to be able to counteract the electrostrictive effect of chloride and sulphate ions on the water structure, so that the density of their aqueous solutions is smaller or only slightly larger than that of water.http://dx.doi.org/10.1155/2014/870106 |
spellingShingle | Giuseppe Graziano Why Do Tetrapropylammonium Chloride and Sulphate Salts Destabilize the Native State of Globular Proteins? The Scientific World Journal |
title | Why Do Tetrapropylammonium Chloride and Sulphate Salts Destabilize the Native State of Globular Proteins? |
title_full | Why Do Tetrapropylammonium Chloride and Sulphate Salts Destabilize the Native State of Globular Proteins? |
title_fullStr | Why Do Tetrapropylammonium Chloride and Sulphate Salts Destabilize the Native State of Globular Proteins? |
title_full_unstemmed | Why Do Tetrapropylammonium Chloride and Sulphate Salts Destabilize the Native State of Globular Proteins? |
title_short | Why Do Tetrapropylammonium Chloride and Sulphate Salts Destabilize the Native State of Globular Proteins? |
title_sort | why do tetrapropylammonium chloride and sulphate salts destabilize the native state of globular proteins |
url | http://dx.doi.org/10.1155/2014/870106 |
work_keys_str_mv | AT giuseppegraziano whydotetrapropylammoniumchlorideandsulphatesaltsdestabilizethenativestateofglobularproteins |