Hydrophobic Interactions in Aqueous Urea Solutions with Implications for the Mechanism of Protein Denaturation-Reference-Cited by-同舟云学术

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Hydrophobic Interactions in Aqueous Urea Solutions with Implications for the Mechanism of Protein Denaturation

Published:1998-01-01 Issue:2 Volume:120 Page:427-428
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Wallqvist A.¹,Covell D. G.¹,Thirumalai D.²

Affiliation:

1. Frederick Cancer Research and Development Center National Cancer Institute Science Applications International Corporation Frederick Maryland 21702

2. Department of Chemistry and Biochemistry Institute for Physical Science and Technology University of Maryland College Park, Maryland 20742

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja972053v

Reference19 articles.

1. On the Conformational Stability of Globular Proteins

2. The Solubility of Amino Acids and Related Compounds in Aqueous Urea Solutions

3. Isothermal Unfolding of Globular Proteins in Aqueous Urea Solutions

4. Nonpolar Group Participation in the Denaturation of Proteins by Urea and Guanidinium Salts. Model Compound Studies

5. Structural Approach to the Solvent Power of Water for Hydrocarbons; Urea as a Structure Breaker

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