Hydrophobic−Hydrophilic Solvation of Variously Substituted N-Alkylureas in Aqueous Solution: A Calorimetric Study at a Temperature of 298.15 K-Reference-Cited by-同舟云学术

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Hydrophobic−Hydrophilic Solvation of Variously Substituted N-Alkylureas in Aqueous Solution: A Calorimetric Study at a Temperature of 298.15 K

Published:2009-09-10 Issue:9 Volume:54 Page:2739-2744
ISSN:0021-9568
Container-title:Journal of Chemical & Engineering Data
language:en
Short-container-title:J. Chem. Eng. Data

Author:

Della Gatta Giuseppe¹,Badea Elena¹,Jóźwiak Małgorzata²,Barone Guido³

Affiliation:

1. Department of Chemistry IFM, University of Turin, via P. Giuria 9, 10125 Torino, Italy

2. Faculty of Chemistry, Physical Chemistry Department, University of Łódź, ul. Pomorska 165, 90−236 Łódź, Poland

3. Department of Chemistry, University Federico II of Naples, Complesso Universitario di Monte S. Angelo, Via Cintia, 80126 Napoli, Italy

Publisher

American Chemical Society (ACS)

Subject

General Chemical Engineering,General Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/je9003405

Reference49 articles.

1. Temperature dependence of the hydrophobic interaction in protein folding.

2. Stability of Protein Structure and Hydrophobic Interaction

3. Contribution of Hydration to Protein Folding Thermodynamics

4. Use of liquid hydrocarbon and amide transfer data to estimate contributions to thermodynamic functions of protein folding from the removal of nonpolar and polar surface from water

5. Coupling of Local Folding to Site-Specific Binding of Proteins to DNA

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