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J Phys Chem C 2012, 116:5420–5426.CrossRef Competing interests The authors declare that they have no competing interests. Authors’ contributions DZ carried out the sample preparation, performed all the analyses, and wrote the paper. YL (Lu), and KQ participated on its https://www.selleckchem.com/products/VX-765.html analysis. HY, CW, CC, CT, YZ, and YL (Luo) directed the research and made corrections to the manuscript. All authors read and approved the final manuscript.”
“Background Over past decades, nanopores have been widely evolved in various devices for investigating unlabeled biopolymers at the single-molecule level [1, 2]. Although the focus is on nucleic acids, proteins are becoming a prime target for investigation [3, 4]. Protein transport through the cellular compartments is a very important physiological process for substance and energy

Selleck AZD6738 metabolism of living cells [5–7]. Compared with DNA sequencing, protein translocation through nanopores is more challenging. First, proteins have a variety of charge profiles depending on the solvent environment. When pH is lower than the isoelectric point of proteins, the net charge of protein is positive, while the reverse case is negatively

charged [8, 9]. Second, each protein has a unique structural architecture, including the primary peptide chain, secondary, tertiary, and quaternary structures, which are responsible for their biological functions. Yet the native protein conformation is only marginally stable. Once the protein’s physical and chemical environment Verteporfin order is modestly changed, the rigid structure of a protein will unfold into random coils [8, 10]. These features of proteins are distinct from the linear DNA with a uniform negative charge. Thus, nanopore experiments on proteins are more complicated than the DNA sequencing. Yet for all that, a set of experiments have demonstrated the unique and advantageous ability of nanopores to discriminate protein translocations [9–14], protein folding [10, 13, 15–18], and enzymatic kinetic reactions [19–26] in the context of single-molecule analysis. For example, nanopores have been used to discriminate the surface charge and size of proteins as a function of pH [27–29]. The unfolding transition and structural stability of proteins have also been studied by chemical and thermal denaturation, as well as electric field stretching [3, 10, 13, 15, 30].