denatured protein

The denatured protein can also bind with the oil in the pan.

However fouling from denatured proteins is still a significant problem.

This eliminates the interactions between the denatured proteins on meat and the oil.

The skin that forms on curdled milk is another common example of denatured protein.

This produces a strong interaction between the denatured proteins and the surface of the container.

Water is also a polar molecule which means, in certain cases, it can bind to the denatured proteins.

If, for example, toxicity is due to denatured proteins, those proteins could be repaired or replaced.

The denatured proteins accumulated inside the ER.

Denatured proteins can exhibit a wide range of characteristics, from loss of solubility to communal aggregation.

Compared to spray drying, drum drying is a more intense heat treatment which results in more denatured proteins.

Alpha-crystallin has chaperone-like properties including the ability to prevent the precipitation of denatured proteins and to increase cellular tolerance to stress.

A fully denatured protein lacks both tertiary and secondary structure, and exists as a so-called random coil.

The entropy of heterogeneous random coil or denatured proteins is significantly higher than that of the folded native state tertiary structure.

It uses gel electrophoresis to separate native proteins by 3-D structure or denatured proteins by the length of the polypeptide.

This Escherichia coli serine endopeptidase is essential for the clearance of denatured proteins from the inner-membrane and periplasmic space.

By temporarily binding to hydrophobic residues exposed by stress, Hsp70 prevents these partially denatured proteins from aggregating, and allows them to refold.

One downside, however, is that complexes may not separate cleanly or predictably, since they cannot move through the polyacrylamide gel as quickly as individual, denatured proteins.

Clostridium histolyticum proteinases, including gamma- and delta-toxin, digest native and denatured proteins to amino acids with the production of ammonia.

It speeds up the degradation of irreversibly denatured proteins and junkproteins by binding to ubiquitinated proteins and to the 26S proteasome.

If elicited antibodies are to be used on membrane blots (proteins subjected to denaturing conditions) then antibodies should be made against denatured proteins.

This potent adjuvant stimulates both cell mediated and humoral immunity with preferential induction of antibody against epitopes of denatured proteins.

These denatured proteins gather together where the air and water meet and create multiple bonds with the other unraveled proteins, and thus become a foam, holding the incorporated air in place.

In vitro it acts as an ATP-independent chaperone by inhibiting protein aggregation and by stabilizing partially denatured proteins, which ensures refolding by the Hsp70-complex.

Petrunkin and Petrunkin (1927, 1928) appear to be the first who studied the binding of GndCl to gelatin and a mixture of thermally denatured protein from brain extract.

Typically, an aggresome forms in response to a cellular stress which generates a large amount of misfolded or partially denatured protein: hyperthermia, overexpression of an insoluble or mutant protein, etc.