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Evaluating unfolding reversibility using temperature cycle measurements

The conformational stability of proteins is of central importance for a large number of commercial products, ranging from biopharmaceutics to industrial enzymes. While conventional stability measurements are routinely performed, e.g., determination of the unfolding temperature, or assessment of long-term stability, little is typically known about the reversibility of the unfolding process. This, however, is an important property of any protein, since an irreversible unfolding eventually leads to reduced long-term stability and thus to poor developability of pharmaceutical or industrial proteins.

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Evaluation of slow equilibration kinetics in antibody chemical denaturation experiments
Evaluation of slow equilibration kinetics in antibody chemical denaturation experiments

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A novel anti-platelet aggregation target of chinensinaphthol methyl ether and neojusticin B obtained from Rostellularia procumbens (L.) Nees
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