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Ribosome-inactivating proteins (RIPs) are separated into the following types based on protein domain composition: [11] Type I (A): RIPs-I are polypeptides composed of an A domain. This is the site of N-glycosidase activity.
Saporin / ˈ s æ p ə r ɪ n / is a protein that is useful in biological research applications, especially studies of behavior. Saporins are so-called ribosome inactivating proteins (RIPs), due to its N-glycosidase activity, from the seeds of Saponaria officinalis (common name: soapwort).
A thermal shift assay (TSA) measures changes in the thermal denaturation temperature and hence stability of a protein under varying conditions such as variations in drug concentration, buffer formulation (pH or ionic strength), redox potential, or sequence mutation. The most common method for measuring protein thermal shifts is differential ...
CEllular Thermal Shift Assay (CETSA ®) is a patented label free chemoproteomics method that has enabled measurements of compound target engagement in intact cells and tissue, without modifications to the target protein. This is accomplished by comparing the measured cellular thermal stability of the protein in the presence and absence of the ...
In a typical assay setup, protein-containing samples are exposed to a ligand of choice, then those samples are aliquoted and heated to separate individual temperature points. Upon binding to a ligand, a protein's thermal stability is expected to increase
A protein mixture is aliquoted into several tubes, which are exposed in parallel to different temperatures and a thermostable protease. The remaining protein can be resolved on SDS-PAGE . Fast parallel proteolysis ( FASTpp ) is a method to determine the thermostability of proteins by measuring which fraction of protein resists rapid proteolytic ...
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Cycloheximide chases are also valuable for assessing how different mutations affect the stability of a protein. Experiments have been conducted in yeast and mammalian cells to determine the critical residues required for protein stability and how disease-associated mutations may be affecting protein half-lives within the cell.