A novel mechanism of “metal gel-shift” by histidine-rich Ni2+-binding Hpn protein from Helicobacter pylori strain SS1

Abstract

Sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) is a universally used method for determining approximate molecular weight (MW) in protein research. Migration of protein that does not correlate with formula MW, termed "gel shifting" appears to be common for histidine-rich proteins but not yet studied in detail. We investigated "gel… (More)
DOI: 10.1371/journal.pone.0172182

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Cite this paper

@inproceedings{Shelake2017ANM, title={A novel mechanism of “metal gel-shift” by histidine-rich Ni2+-binding Hpn protein from Helicobacter pylori strain SS1}, author={Rahul Mahadev Shelake and Yuki Ito and Junya Masumoto and Eugene Hayato Morita and Hidenori Hayashi}, booktitle={PloS one}, year={2017} }