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One example is the use of chloramphenicol acetyl transferase (CAT) to monitor protein folding based on chloramphenicol resistance [26].
Fundamentally, these results indicate that for sdAb, fluorescence intensity is a poor metric to monitor protein folding, with the actual CD spectra providing a more precise Tm.
H N HSQC NMR spectroscopy is widely employed to monitor protein folding characteristics and solution behavior, and the spectra are often termed the "fingerprint" of the protein for their sensitivity to any change in conformation, environment, or interaction.
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It is expected to have many potential applications in protein engineering and research, which include fluorescent labeling for monitoring protein folding, location, and trafficking in cells, and biotinylation for protein immobilization on streptavidin-coated surfaces including protein microchips.
Adding a fluorophore to the C-terminus of a protein, both in solution and on the membrane surface of a live cell, can be a useful tool for monitoring protein folding, location, and trafficking in cells.
The last advances in several approaches, which use NMR: (i) to monitor the protein folding pathway and/or, (ii) to characterize the structure of the intermediate states in such reaction are reviewed in this work.
Researchers have identified the cellular components that monitor the protein folding conditions inside the ER.
As minichaperone is less complex, and does not require high energy co-factors like ATP, for its function as compared to conventional GroEL-GroES system, it can act as a very good in vitro as well as in vivo chaperone model for monitoring assisted protein folding phenomenon.
The unfolded protein response (UPR) monitors the protein folding capacity of the endoplasmic reticulum (ER).
The molecular gatekeepers of the UPR are ER-resident transmembrane proteins that monitor the quality of protein folding in the ER and relay that information to the rest of the cell.
It is executed by proteins called molecular chaperones, which assist in protein folding, monitor and maintain structural protein integrity, refold misfolded proteins, disentangle aggregated proteins, and target proteins for degradation.
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