The effect of urea on aqueous hydrophobic contact-pair interactions.
Phys Chem Chem Phys
; 15(1): 213-22, 2013 Jan 07.
Article
em En
| MEDLINE
| ID: mdl-23160346
ABSTRACT
Urea is perhaps the most common denaturant used for studying proteins. However the mechanism of denaturation is still not well understood. Recent theoretical work suggests that van der Waals interactions between urea and non-polar amino acid residues are a major contributor to the protein denaturation process. However, there are few experimental data measuring the effect of urea on hydrophobic interactions. In this work we have determined how the addition of urea to the aqueous solvent affects the contact-pair formed between alkyl and phenyl groups in model compounds the data indicate that for solutes having a radius smaller than 2.87 Å cavity formation energetics dominate, therefore the addition of urea promotes the formation of hydrophobic contact pairs; while for larger solutes, van der Waals interactions have the largest magnitude, causing urea to disrupt the formation of contact pairs. The influence of urea on hydrophobic interactions is shown to be continuous in the 1-8 M concentration range and is well-correlated with the predictions of scaled particle theory. This demonstrates that the effect of urea on hydrophobic contact pairs can be explained by the changes observed in the solvent packing density, without having to invoke changes in the hydrogen bonding network of water.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Ureia
Tipo de estudo:
Prognostic_studies
Idioma:
En
Revista:
Phys Chem Chem Phys
Assunto da revista:
BIOFISICA
/
QUIMICA
Ano de publicação:
2013
Tipo de documento:
Article
País de afiliação:
Canadá