Recommanded Product: 1539-42-0In 2021 ,《Going the dHis-tance: Site-Directed Cu2+ Labeling of Proteins and Nucleic Acids》 was published in Accounts of Chemical Research. The article was written by Gamble Jarvi, Austin; Bogetti, Xiaowei; Singewald, Kevin; Ghosh, Shreya; Saxena, Sunil. The article contains the following contents:
Conspectus: In this Account, we showcase site-directed Cu2+ labeling in proteins and DNA, which has opened new avenues for the measurement of the structure and dynamics of biomols. using ESR (EPR) spectroscopy. In proteins, the spin label is assembled in situ from natural amino acid residues and a metal complex and requires no post-expression synthetic modification or purification procedures. The labeling scheme exploits a double histidine (dHis) motif, which utilizes endogenous or site-specifically mutated histidine residues to coordinate a Cu2+ complex. Pulsed EPR measurements on such Cu2+-labeled proteins potentially yield distance distributions that are up to 5 times narrower than the common protein spin label-the approach, thus, overcomes the inherent limitation of the current technol., which relies on a spin label with a highly flexible side chain. This labeling scheme provides a straightforward method that elucidates biophys. information that is costly, complicated, or simply inaccessible by traditional EPR labels. Examples include the direct measurement of protein backbone dynamics at β-sheet sites, which are largely inaccessible through traditional spin labels, and rigid Cu2+-Cu2+ distance measurements that enable higher precision in the anal. of protein conformations, conformational changes, interactions with other biomols., and the relative orientations of two labeled protein subunits. Likewise, a Cu2+ label has been developed for use in DNA, which is small, is nucleotide independent, and is positioned within the DNA helix. The placement of the Cu2+ label directly reports on the biol. relevant backbone distance. Addnl., for both of these labeling techniques, we have developed models for interpretation of the EPR distance information, primarily utilizing mol. dynamics (MD) simulations. Initial results using force fields developed for both protein and DNA labels have agreed with exptl. results, which has been a major bottleneck for traditional spin labels. Looking ahead, we anticipate new combinations of MD and EPR to further our understanding of protein and DNA conformational changes, as well as working synergistically to investigate protein-DNA interactions. In addition to this study using Bis(pyridin-2-ylmethyl)amine, there are many other studies that have used Bis(pyridin-2-ylmethyl)amine(cas: 1539-42-0Recommanded Product: 1539-42-0) was used in this study.
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