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Description
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The plasmid MspA-H is designed for the preparation of a mutant Mycobacterium smegmatis porin A (MspA) protein nanopore, which is engineered with a histidine at the site 91. MspA nanopore is a channel-forming protein that allows small hydrophilic nutrients to enter the bacterium. Its crystal structure has been characterized using X-ray diffraction (Science, 2004, 303, 1189-1192). The engineered MspA nanopore ( Proc. Natl. Acad. Sci. , 2008, 105, 20647-20652) is widely applied for DNA sequencing (Nat. Biotechnol., 2012, 30, 349-353) because its geometry (1 nm-long, 1.2 nm-wide constriction) provides high spatial resolution. Recently, MspA is also verified to be an excellent nanopore for single-molecule reaction (Nat. Commun, 2019, 10, 5668). In our work, the MspA-H nanopore is designed for coordination study at the single-molecule level. The most sensitive site 91 (the narrowest restriction-1.2 nm wide) of MspA is mutated to the histidine which acts as the coordination site. The coordination reaction between the histidine residue and single monatomic metal ions is systematically studied. The coordination principle in the confined space is unraveled (Chem. Sci., 2020, DOI: 10.1039/C9SC05260G).
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