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Direct measurement of protein electrostatic interactions in cells

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摘要 Recently, a detailed nuclear magnetic resonance (NMR) study was performed on the fate of exposed/surface charge pairs ina protein on transferring it from a test tube to cytoplasmic soup [10], in which the authors directly measured the proteinelectrostatic interactions and elucidated the influencing factors in cells (https://doi.org/10.1021/jacs.1c10154).Protein electrostatic interactions are a kind of non-covalent interactions between charged amino acid residues [1e4]. Inorganisms, electrostatic interactions play vital roles in many important biological processes, such as enzyme catalysis,protein protein interactions, and protein DNA/RNA interactions. Studies of electrostatic interactions of proteins wereconventionally carried out in buffers rather than in cells. However, the influence of the high macromolecular concentration(up to 450 g/L) [5] in cells on protein folding, stability, and interactions is nonnegligible [6e9]. Accurate measurement andanalysis of electrostatic interactions under the influence of cellular environments are highly desired to understand thephysiochemistry and functions of proteins in cells.
作者 Dong Long
出处 《Magnetic Resonance Letters》 2022年第1期59-60,I0003,共3页 磁共振快报(英文)
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