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This presents a limitation if the turnover of a particularly stable protein is being studied. Additionally, cycloheximide chases only offer the ability to look at steady state proteins levels as opposed to newly translated protein levels such as with pulse chase. Therefore, only protein degradation and not protein maturation is able to be observed.
Thermostable proteins are often more useful than their non-thermostable counterparts, e.g., DNA polymerase in the polymerase chain reaction, [7] so protein engineering often includes adding mutations to increase thermal stability. Protein crystallization is more successful for proteins with a higher melting point [8] and adding buffer ...
These interactions include salt bridges and hydrogen bonds. Salt bridges are unaffected by high temperatures, therefore, are necessary for protein and enzyme stability. A third force used to increase thermostability in proteins and enzymes is the presence of disulfide bonds. They present covalent cross-linkages between the polypeptide chains.
In the less extensive technique of equilibrium unfolding, the fractions of folded and unfolded molecules (denoted as and , respectively) are measured as the solution conditions are gradually changed from those favoring the native state to those favoring the unfolded state, e.g., by adding a denaturant such as guanidinium hydrochloride or urea.
Binding of a drug to a protein often leads to ligand-induced stabilization of the protein (1), which can be measured by comparing the amount of non-denatured protein remaining in a drug-treated sample to an untreated control. The change in protein stability can be visualized as a rightward shift in its stability curve (2).
The new level may be higher than the initial level (hypertrophy) in the case of strength training or lower in the case of dieting or disuse atrophy. This adjustment contributes to homeostasis but does not require feedback regulation. Gradual, asymptotic approach to a new balance between synthesis and degradation produces a stable level.
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