Examples of 'denatured proteins' in a sentence
Meaning of "denatured proteins"
denatured proteins - Denatured proteins are proteins that have undergone a structural change, typically due to external factors such as heat, pH extremes, or chemical exposure. This alteration in structure can lead to loss of function or biological activity in the protein
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denatured proteins
Denatured proteins are proteins that have been broken down.
Metabolism of proteins and the removal of denatured proteins.
Denatured proteins adhere to surfaces and are difficult to remove.
The antibodies are specific to the native or denatured proteins.
However fouling from denatured proteins is still a significant problem.
Denatured proteins were removed by centrifugation.
The proteinase digests the denatured proteins into smaller fragments.
Denatured proteins are generally insoluble and precipitate out of a solution.
The protein solution to be acidified is preferably substantially free of denatured proteins.
The protected peptides or denatured proteins are particularly useful for administration by mouth.
The suspension is then cooled and centrifuged to precipitate the denatured proteins.
Remember that certain isolates contain denatured proteins that make the supplement ineffective.
The denatured proteins and peptides lose their inherent physiochemical properties and physiological activity.
Their role could be the elimination of substances such as denatured proteins of the chloroplasts.
Any denatured proteins which do form during processing are excluded from the product during ultrafiltration.
See also
Methods are known for oxidizing and refolding denatured proteins into an active state.
Upon cooling, denatured proteins are susceptible to aggregate to form insoluble precipitates.
IBs are essentially made of denatured proteins.
Alkylation of the denatured proteins using at least one alkylating agent ;.
This system additionally requires ATP to refold denatured proteins.
Denatured proteins can exhibit a wide range of characteristics, from loss of solubility to protein aggregation.
HSPs are chaperones involved in the folding of newly synthesized and denatured proteins.
Consequently, the denatured proteins lose intrinsic physicochemical properties and physiologically active effects.
The disulfide bond enhances BiP 's binding to denatured proteins.
Denatured proteins lose their 3D structure and therefore can not function.
They help prevent protein unfolding and help re-fold denatured proteins.
Soluble protein was separated from aggregated denatured proteins by centrifugation at 4°C for ten minutes.
Currently, this drying intensity is measured by the turbidity of the solution of denatured proteins.
The denatured proteins may be in the form of inclusion bodies ( IBs ).
Thus, any wash solution capable of removing denatured proteins can be used.
The denatured proteins were removed by centrifugation to obtain a crude enzyme solution of hydantoinase ( 1,100 units / ml ).
After cooling, an insoluble precipitate phase containing denatured proteins and other debris will develop.
The extract resulting from alkaline treatment above contained glycosaminoglycan, alkali, denatured proteins and salts.
Compact layer 175 is composed primarily of denatured proteins present in tissue and blood.
The small nitrogen bubbles provide a large interface, which allows the denatured proteins to coagulate.
In contrast, T-cells can not distinguish between native and denatured proteins.
Alternatively, 10 % glycerol was added to the denatured proteins.
Gel-electrophoresis demonstrated a clear difference in the mobility of non-denatured and denatured proteins ( see Figure 11 ).
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