The denaturation of proteins

The Denaturation and Hydration of Proteins. I*

Of the different kinds of denaturation of proteins, that by heat has been investigated most thoroughly. The theory has been put forward that the loss of the zwitter ion structure by an interaation of the ionogenic groups is the most important of the electrochemical changes which a protein undergoes by the action of heat (Pauli (6), Cohn (2)). The question as to whether other structural changes ...

Xxi . the Denaturation of Proteins . Vi .

Folding kinetics of proteins and cold denaturation.

Folding kinetics of a lattice model of protein is studied. It uses the random energy model for the intrachain couplings and a temperature dependent free energy of solvation derived from a realistic hydration model of apolar solutes. The folding times are computed using Monte Carlo simulations in the region of the phase diagram where the chain occurs in the native structure. These folding times ...

On the structural stability and solvent denaturation of proteins. II. Denaturation by the ureas.

The effects of the water-miscible straight chain and branched alcohols and glycols on the native conformation of sperm whale myoglobin, cytochrome c, and oc-chymotrypsinogen have been investigated by spectral, difference spectral, and optical rotatory dispersion methods. Based on the midpoints of the denaturation transitions, that is, the amount of alcohol or glycol required to produce 50% dena...

Nature of Heat Denaturation of Proteins

Chick and Martin (1) have shown that the heat coagulation of proteins consists of two distinct processes; tiiz., (a) denaturation, the alteration of the protein under the influence of heat, and (b) agglutination, the separation of the altered protein in a particulate form. Agglutination, in which hydrogen ion concentration and electrolyte contents play important roles (2), is now a fairly well ...