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PRIME (PRobe Incorporation Mediated by Enzymes) : ウィキペディア英語版 | PRIME (PRobe Incorporation Mediated by Enzymes) PRIME (PRobe Incorporation Mediated by Enzymes) is a molecular biology research tool developed by Alice Y. Ting and the Ting Lab at MIT for site-specific labeling of proteins in living cells with chemical probes. Probes often have useful biophysical properties, such as fluorescence, and allow imaging of proteins.〔 Ultimately, PRIME enables scientists to study functions of specific proteins of interest. == Significance == Protein labeling with fluorescent molecules allows the visualization of protein dynamics, localization, and protein-protein interactions, and therefore serves as an important technique to understand protein functions and networks in living cells. The protein labeling should have a high selectivity towards the protein of interest, and should not interfere with the natural functions of the protein. Although genetic coding of fluorescent proteins, such as the green fluorescent protein (GFP), is the most popular technique due to its high specificity, fluorescent proteins are likely to interfere with the functions of the protein to which they are fused because of their large sizes.〔 There are multiple tagging tools, such as HaloTag, SNAP tag, and FlAsH, developed in order to overcome the weakness of traditional protein labeling with fluorescent proteins. However, they still have significant shortcomings either due to the large size of a tag or the low specificity of the labeling process. PRIME has been developed in order to achieve a high labeling specificity comparable to fluorescent proteins with small molecules.〔
抄文引用元・出典: フリー百科事典『 ウィキペディア(Wikipedia)』 ■ウィキペディアで「PRIME (PRobe Incorporation Mediated by Enzymes)」の詳細全文を読む
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