One of the characteristic manifestations of biological activity of proteins resides in their ability to elicit antibody formation. While the activity of certain immune bodies, as well as that of enzymes, or viruses, is known to be destroyed by processes causing protein denaturation, the relation between denaturation and antigenicity is only vaguely understood. I t has been reported that denatur...

Fluorescence of green fluorescent protein mutant, 2-5 GFP is observed during denaturation by guanidine. The fluorescence intensity decreases exponentially but the fluorescence lifetime does not change during denaturation. The fluorescence lifetime of the denatured protein is shorter than that of native form. As the protein structure is modified by guanidine, solvent water molecules penetrate in...

The partial-denaturation map of T4 DNA is obtained by using benzyldodecyldimethyl ammonium chloride in the presence of a high concentration of formamide. In this way suitable conditions for preparation of electron microscope specimens and partial denaturation within a temperature range low enough to minimize the endonucleolytic cleavage, are realized. It is found that, under our experimental co...

Urea and guanidine hydrochloride (GdnHCl) denaturation of bovine serum albumin (BSA) were investigated using bromophenol blue (BPB) binding as a probe. Addition of BPB to BSA produced an absorption difference spectrum in the wavelength range, 525-675 nm with a minimum at 587 nm and a maximum at 619 nm. The magnitude of absorption difference (DeltaAbs.) at 619 nm decreased on increasing urea/Gdn...

UNLABELLED Recently developed proteomic technologies allow to profile thousands of proteins within a high-throughput approach towards biomarker discovery, although results are not as satisfactory as expected. In the present study we demonstrate that serum proteome denaturation is a key underestimated feature; in fact, a new differential denaturation protocol better discriminates serum proteins ...

Cold denaturation is a general property of globular proteins, but it is difficult to directly characterize because the transition temperature of protein cold denaturation, T(c), is often below the freezing point of water. As a result, studies of protein cold denaturation are often facilitated by addition of denaturants, using destabilizing pHs or extremes of pressure, or reverse micelle encapsu...

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 ...

We elucidate the mechanism of cold denaturation through constant-pressure simulations for a model of hydrophobic molecules in an explicit solvent. We find that the temperature dependence of the hydrophobic effect induces, facilitates, and is the driving force for cold denaturation. The physical mechanism underlying this phenomenon is identified as the destabilization of hydrophobic contact in f...

Two-dimensional infrared correlation spectroscopy (2D-IR) was applied to the study of urea- and heat-induced unfolding denaturation of sarcoplasmic reticulum Ca(2+)-ATPase (SR ATPase). Urea at 2-3 M causes reversible loss of SR ATPase activity, while higher concentrations induce irreversible denaturation. Heat-induced denaturation is a non-two-state process, with an "intermediate state" (at t a...

background tyrosinase, as a copper-containing enzyme, is widely distributed in different levels of life span. it is also a key enzyme in melanin biosynthesis, which plays a crucial role in determining the color of mammalian skin and hair. objectives the current study aimed to determine the effect of a palladium complex on cresolase and catecholase reactions of mushroom tyrosinase (mt). material...