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dc.contributor.authorJaiswal N.-
dc.contributor.authorRaikwal N.-
dc.contributor.authorPandey H.-
dc.contributor.authorAgarwal N.-
dc.contributor.authorArora A.-
dc.contributor.authorPoluri, Krishna Mohan-
dc.contributor.authorKumar D.-
dc.identifier.citationMagnetic Resonance in Chemistry(2018), 56(4): 285-299-
dc.description.abstractHelicobacter pylori (H. pylori) colonizes under harsh acidic/oxidative stress conditions of human gastrointestinal tract and can survive there for infinitely longer durations of host life. The bacterium expresses several harbinger proteins to facilitate its persistent colonization under such conditions. One such protein in H. pylori is histone-like DNA binding protein (Hup), which in its homo-dimeric form binds to DNA to perform various DNA dependent cellular activities. Further, it also plays an important role in protecting the genomic DNA from oxidative stress and acidic denaturation. Legitimately, if the binding of Hup to DNA is suppressed, it will directly impact on the survival of the bacterium, thus making Hup a potential therapeutic target for developing new anti-H. pylori agents. However, to inhibit the binding of Hup to DNA, it is necessary to gain detailed insights into the molecular and structural basis of Hup-dimerization and its binding mechanism to DNA. As a first step in this direction, we report here the nuclear magnetic resonance (NMR) assignments and structural features of Hup at pH 6.0. The study revealed the occurrence of dynamic equilibrium between its monomer and dimer conformations. The dynamic equilibrium was found to shifting towards dimer both at low temperature and low pH; whereas DNA binding studies evidenced that the protein binds to DNA in its dimeric form. These preliminary investigations correlate very well with the diverse functionality of protein and will form the basis for future studies aiming to develop novel anti-H. pylori agents employing structure-based-rational drug discovery approach. Copyright © 2017 John Wiley & Sons, Ltd.-
dc.publisherJohn Wiley and Sons Ltd-
dc.relation.ispartofMagnetic Resonance in Chemistry-
dc.subjectHelicobacter pylori-
dc.subjecthistone like DNA binding protein-
dc.subjectmultiple conformations-
dc.subjectNMR resonance assignments-
dc.subjectsecondary structure-
dc.titleNMR elucidation of monomer–dimer transition and conformational heterogeneity in histone-like DNA binding protein of Helicobacter pylori-
dc.affiliationJaiswal, N., Centre of Biomedical Research, SGPGIMS Campus, Lucknow, 226014, India, Dr. APJ Abdul Kalam Technical University, IET Campus, Sitapur Road, Lucknow, Uttar Pradesh 226021, India-
dc.affiliationRaikwal, N., Centre of Biomedical Research, SGPGIMS Campus, Luc-
dc.description.fundingWe thank the Government of India for providing financial support to the National Facility for High Field NMR at the CBMR, Lucknow. D. K. and P. M. K. acknowledge SERB DST, India for providing him the research grant under EMR Scheme (Registration Number: E-
dc.description.correspondingauthorJaiswal, N.; Centre of Biomedical Research, SGPGIMS Campus, India; email:
Appears in Collections:Journal Publications [BT]

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