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Investigation of metal-binding proteins for bioremediation potential with reference to Hpn, a nickel-binding protein from Helicobacter pyroli strain SS1 (2014-2017)
Exploring the molecular mechanisms of metal ion sensing in cyanobacteria towards bioremediation of heavy metals from the contaminated sites (2010-2014)
Effect of growth hormones on grapefruit at various development stages of berry (2009-2010)
Enhancing nutrient use efficiency through transgenic approaches in rice (2008-2009)
Tissue culture strategies for hill banana (Musa spp., genome - AAB) varieties through male inflorescence: a new approach towards virus (Banana Bunchy Top Virus, BBTV)-free plantlet production (2006-2008)
Probable interrelationship between the differential electrophoretic mobility of Hpn protein and Ni2+ binding
Hpn may not have a definite form in the absence of Ni2+ (A). After denaturation (B), smaller amounts of SDS binding/stacking behavior/larger hydrodynamic radius as well as a combination of some or all of these conditions (C) might have resulted in slower migration on SDS-PAGE (scheme highlighted with yellow background). Ni2+-treated Hpn forms a more compact structure (D). Pictorial structure of metalated Hpn is drawn to explain the model. MALDI spectra showed a partial Ni2+ bound form (E) in denatured SDS-PAGE. Altered binding of SDS (F) caused by replacement of protein-protein to protein-SDS contacts (inhibiting stacking behavior) and/or degree of compactness (or reduced hydrodynamic radius) may be key factors responsible for “metal gel-shift” (scheme highlighted with green background). β-ME, β-mercaptoethanol; EDTA, ethylene diaminetetraacetic acid.
A novel mechanism of “metal gel-shift” by histidine-rich Ni2+-binding Hpn protein from Helicobacter pylori strain SS1. PloS one 12 (2), e0172182.
DOI: https://doi.org/10.1371/journal.pone.0172182
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