Why Do Tetrapropylammonium Chloride and Sulphate Salts Destabilize the Native State of Globular Proteins?
Author
Source
Issue
Vol. 2014, Issue 2014 (31 Dec. 2014), pp.1-4, 4 p.
Publisher
Hindawi Publishing Corporation
Publication Date
2014-01-27
Country of Publication
Egypt
No. of Pages
4
Main Subjects
Medicine
Information Technology and Computer Science
Abstract EN
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.
American Psychological Association (APA)
Graziano, Giuseppe. 2014. Why Do Tetrapropylammonium Chloride and Sulphate Salts Destabilize the Native State of Globular Proteins?. The Scientific World Journal،Vol. 2014, no. 2014, pp.1-4.
https://search.emarefa.net/detail/BIM-1051423
Modern Language Association (MLA)
Graziano, Giuseppe. Why Do Tetrapropylammonium Chloride and Sulphate Salts Destabilize the Native State of Globular Proteins?. The Scientific World Journal No. 2014 (2014), pp.1-4.
https://search.emarefa.net/detail/BIM-1051423
American Medical Association (AMA)
Graziano, Giuseppe. Why Do Tetrapropylammonium Chloride and Sulphate Salts Destabilize the Native State of Globular Proteins?. The Scientific World Journal. 2014. Vol. 2014, no. 2014, pp.1-4.
https://search.emarefa.net/detail/BIM-1051423
Data Type
Journal Articles
Language
English
Notes
Includes bibliographical references
Record ID
BIM-1051423