Could denaturation of proteins.
نویسندگان
چکیده
منابع مشابه
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 ...
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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 ...
متن کاملTheory of cold denaturation of proteins
A new approach to the problem of cold denaturation is presented. It is based on solvent-induced effects operating on hydrophilic groups along the protein. These effects are stronger than the corresponding hydrophobic effects, and they operate on the hydrophilic groups which are plentiful than hydrophobic groups. It is shown that both heat and cold denaturation can be explained by these hydrophi...
متن کاملThermal Denaturation Equilibria of Tmv Coat Proteins
Thermal denaturation of RNA free coat proteins of tobacco mosaic virus (TMV) was studied for wildtype TMV (vulgare) and the temperature-sensitive mutant, Ni 118. The ability to form soluble aggregates as well as the optical properties (ORD, UV-difference spectra), and the sedimen tation behavior were used as criteria for the native state. At pH 7.5 , 7 = 0 .0 2 denaturation is reversible for b...
متن کاملCold and warm denaturation of proteins.
We introduce a simplified protein model where the water degrees of freedom appear explicitly (although in an extremely simplified fashion). Using thismodel we are able to recover both the warm and the cold protein denaturation within a single framework, while addressing important issues about the structure of model proteins.
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ژورنال
عنوان ژورنال: Seibutsu Butsuri
سال: 1995
ISSN: 0582-4052,1347-4219
DOI: 10.2142/biophys.35.40