7-days of FREE Audio papers, translation & more with Prime
7-days of FREE Prime access
7-days of FREE Audio papers, translation & more with Prime
7-days of FREE Prime access
https://doi.org/10.1039/b302893c
Copy DOIJournal: Phys. Chem. Chem. Phys. | Publication Date: Jan 1, 2003 |
Citations: 9 |
The effects of added protein denaturant (urea) on the volumetric and thermochemical properties of several protein model compounds (cyclic dipeptides) have been investigated at T = 298.15 K and p = 0.1 MPa. Relative densities and specific heat capacities are reported for the cyclic dipeptides cyclo-glycylglycine, cyclo-alanylalanine and cyclo-sarcosylsarcosine in aqueous urea solutions in the concentration range 1 ≤ m(urea)/mol kg−1 ≤ 11. The measurements were performed using a Sodev O2D vibrating tube densimeter and a Picker dynamic microcalorimeter. Apparent molar volumes and heat capacities have been calculated and their concentration dependences have been modeled to give partial molar properties at infinite dilution. The partial molar properties have been used to calculate thermodynamic parameters describing the transfer of the cyclic dipeptides from water to aqueous urea solutions. Estimates of transfer properties for the glycyl group and the alanyl side chain have been obtained using the principles of group additivity. The interaction of urea with the investigated protein model compounds is discussed in terms of the role of urea as a protein denaturant.
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.