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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.
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.
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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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 ...
In a 2024 survey of Americans’ food behavior conducted by the International Food Information Council, 71% said they want to increase their protein intake, compared to 67% in 2023 and just 59% in ...
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