Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction

https://www.biosyn.com/Images/ArticleImages/pdf/A%20simple.pdf

A simple method for displaying the hydropathic character of a protein

The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis

Intermolecular interactions from a natural bond orbital, donor-acceptor viewpoint

http://www.real-times.com.cn/guest/20143219541398.pdf

Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa.

Physical Chemistry of Macromolecules

The Solubility of Hydrocarbons in Water. Solubility of Amphiphiles in Water and Organic Solvents. The Effect of Temperature: Anomalous Entropy and Heat Capacity. The Structure of Water. Micelles: Introduction. Thermodynamics of Micelle Formation. Micelle Size and Shape. Mixed Micelles. Monolayers. Biological Lipids. Motility and Order. Proteins: Hydrophobic Side Chains and Conformational Change. The Association of Hydrocarbons and Amphiphiles with Common Soluble Proteins. Serum Lipoproteins. Biological Membranes. Membrane Proteins. Author and Subject Indices.

The Hydrophobic Effect: Formation of Micelles and Biological Membranes

The hydrophobic effect

Publisher Summary This chapter reviews theoretical models that may be constructed and equations that may be derived from them to understand the process of protein denaturation. Given that the native state is stable under physiological conditions, the question arises whether the effects of environmental changes on the equilibrium between native and denatured states can be predicted, so as to account for the loss of stability of the native state and the appearance of different denatured states under specified conditions. This question involves not the absolute values for the free energies and other thermodynamic parameters for denaturation processes, but the changes in these parameters, along with changes in environmental variables. These changes can be predicted semiquantitatively. Furthermore, one can account both for the products formed under different conditions and for the character of the transitions from native to denatured state, at least for the simple proteins that have been studied in detail.

Protein denaturation. C. Theoretical models for the mechanism of denaturation.

http://staff.ustc.edu.cn/~liuyz/methods/AA_solubility.pdf

Charles Tanford

Papers

Physical Chemistry of Macromolecules

The Hydrophobic Effect: Formation of Micelles and Biological Membranes

The hydrophobic effect

Protein denaturation. C. Theoretical models for the mechanism of denaturation.

The Solubility of Amino Acids and Two Glycine Peptides in Aqueous Ethanol and Dioxane Solutions ESTABLISHMENT OF A HYDROPHOBICITY SCALE