collagen, which is widely distributed in pluricellular animals, is one of the most fundamental constituents of the extracellular matrix, and plays mechanically or physiologically important roles in their bodies. in this study, the biochemical and physical characteristics of pepsin-solubilized collagen from the mantle of yesso scallop (ympc), a by-product of processing, was determined. electroph...

Proteins denature not only at high, but also at low temperature as well as high pressure. These denatured states are not easily accessible for experiment, because usually heat denaturation causes aggregation, whereas cold or pressure denaturation occurs at temperatures well below the freezing point of water or pressures above 5 kbar, respectively. Here we have obtained atomic details of the pre...

Crystalline soybean trypsin inhibitor protein undergoes denaturation on heating which is reversed on cooling. In the range of temperature of 35 to 50 degrees C. a solution of the protein consists of a mixture of native and denatured forms in equilibrium with each other. The equilibrium is only slowly established and its final value at any temperature is the same whether a heated, denatured solu...

The coagulation of isoelectric egg albumin solutions, on exposure to ultraviolet radiation, involves three distinct processes, (1) the light denaturation of the albumin molecule, (2) a reaction between the light denatured molecule and water which may be similar to heat denaturation but occurs at a lower temperature, and (3), the flocculation of the denatured molecules to form a coagulum. The li...

Recent theoretical predictions on DNA mechanical separation induced by pulling forces are numerically tested within a model in which self-avoidance for DNA strands is fully taken into account. DNA strands are described by interacting pairs of self avoiding walks (SAW) which are pulled apart by a force applied at the two extremities. The whole phase diagram is spanned by extensive Monte Carlo (M...

Protein denaturation is considered to be the main reason for both water loss and textural changes in fish during thermal processing. Denaturation of proteins in muscle of farmed Atlantic cod was studied by differential scanning calorimetry. The denaturation of the proteins was compared to cook loss and loss in water holding capacity and it was shown that the protein denaturation occurs in a low...

The extent of urea denaturation depends on the concentration of protein and urea and also on the temperature of the solution. Egg albumin solutions (0.9 per cent) are not denatured by 20 per cent urea, denature slowly with 25 per cent urea, and denature rapidly with 35 per cent urea at room temperature. At a higher temperature 30 per cent urea is rapidly effective. Denaturation of the egg album...

The effect of temperature and calcium ions on the denaturation of a recombinant alpha-amylase from Bacillus halmapalus alpha-amylase (BHA) has been studied using calorimetry. It was found that thermal inactivation of BHA is irreversible and that calcium ions have a significant effect on stability. Thus an apparent denaturation temperature ( T (d)) of 83 degrees C in the presence of excess calci...

the interaction between nano-sio2 and lysozyme was investigated by the method of uv-visible  detection and fluorescence spectroscopic techniques. the thermal denaturation of lysozyme has been investigated in the presence and absence of nano-sio2 over the temperature range (293-373) k in different buffers and ph values, using temperature scanning spectroscopy. the presence of nano-sio2 caused th...