Mechanism of the interactions of aliphatic alcohols with bovine serum albumin in the ternary systems—1H n.m.r. study: 1. Aqueous solutions BSA-alcohols-urea
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,General Medicine,Biochemistry,Structural Biology
Reference18 articles.
1. THE STRUCTURE OF WATER AND HYDROPHOBIC BONDING IN PROTEINS. III. THE THERMODYNAMIC PROPERTIES OF HYDROPHOBIC BONDS IN PROTEINS1,2
2. Proton nuclear magnetic resonance study of the association of monovalent and divalent alcohols with bovine serum albumin
3. The Relationship of Structure to the Effectiveness of Denaturing Agents for Proteins
4. Denaturation of Globular Proteins
5. The Effect of Compounds of the Urea-Guanidinium Class on the Activity Coefficient of Acetyltetraglycine Ethyl Ester and Related Compounds1
Cited by 3 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献
1. Role of aliphatic alcohols on the stability of rat-tail tendon (RTT) collagen fiber;Journal of Polymer Science Part B: Polymer Physics;1999-07-01
2. Association of monoalkylureas with bovine serum albumin: 1H n.m.r. study;International Journal of Biological Macromolecules;1986-10
3. Mechanism of the interaction of aliphatic alcohols with bovine serum albumin in the ternary systems—1H n.m.r. study: 2. Aqueous solutions BSA-alcohols-sulphonamides;International Journal of Biological Macromolecules;1985-08
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