Jain, Rohit

[["dc.bibliographiccitation.firstpage","1855"],["dc.bibliographiccitation.issue","10-12"],["dc.bibliographiccitation.journal","Zeitschrift für physikalische Chemie"],["dc.bibliographiccitation.lastpage","1867"],["dc.bibliographiccitation.volume","229"],["dc.contributor.author","Yin, Z."],["dc.contributor.author","Rajkovic, Ivan"],["dc.contributor.author","Veedu, Sreevidya Thekku"],["dc.contributor.author","Deinert, Sascha"],["dc.contributor.author","Raiser, Dirk"],["dc.contributor.author","Jain, Rohit"],["dc.contributor.author","Fukuzawa, Hironobu"],["dc.contributor.author","Wada, Shin-ichi"],["dc.contributor.author","Quevedo, Wilson"],["dc.contributor.author","Kennedy, Brian"],["dc.contributor.author","Schreck, Simon"],["dc.contributor.author","Pietzsch, Annette"],["dc.contributor.author","Wernet, Philippe"],["dc.contributor.author","Ueda, Kyoshi"],["dc.contributor.author","Foehlisch, Alexander"],["dc.contributor.author","Techert, Simone"],["dc.date.accessioned","2018-11-07T10:02:46Z"],["dc.date.available","2018-11-07T10:02:46Z"],["dc.date.issued","2015"],["dc.description.abstract","X-ray spectroscopy is a powerful tool to study the local charge distribution of chemical systems. Together with the liquid jet it becomes possible to probe chemical systems in their natural environment, the liquid phase. In this work, we present X-ray absorption (XA), X-ray emission (XE) and resonant inelastic X-ray scattering (RIXS) data of pure water and various salt solutions and show the possibilities these methods offer to elucidate the nature of ion-water interaction."],["dc.identifier.doi","10.1515/zpch-2015-0610"],["dc.identifier.isi","000364609000021"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/38298"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.relation","SFB 1073: Kontrolle von Energiewandlung auf atomaren Skalen"],["dc.relation","SFB 1073 | Topical Area C | C02 In situ hochauflösende Untersuchung des aktiven Zustands bei der photo- und elektrochemischen Wasserspaltung"],["dc.relation.issn","0942-9352"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.workinggroup","RG Techert (Structural Dynamics in Chemical Systems)"],["dc.title","Ionic Solutions Probed by Resonant Inelastic X-ray Scattering"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","81"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","European Biophysics Journal"],["dc.bibliographiccitation.lastpage","89"],["dc.bibliographiccitation.volume","45"],["dc.contributor.author","Jain, Rohit"],["dc.contributor.author","Khan, Nazimuddin"],["dc.contributor.author","Menzel, Andreas"],["dc.contributor.author","Rajkovic, Ivan"],["dc.contributor.author","Konrad, Manfred"],["dc.contributor.author","Techert, Simone"],["dc.date.accessioned","2018-11-07T10:21:32Z"],["dc.date.available","2018-11-07T10:21:32Z"],["dc.date.issued","2016"],["dc.description.abstract","Bio-catalysis is the outcome of a subtle interplay between internal motions in enzymes and chemical kinetics. Small-angle X-ray scattering (SAXS) investigation of an enzyme's internal motions during catalysis offers an integral view of the protein's structural plasticity, dynamics, and function, which is useful for understanding allosteric effects and developing novel medicines. Guanylate kinase (GMPK) is an essential enzyme involved in the guanine nucleotide metabolism of unicellular and multicellular organisms. It is also required for the intracellular activation of numerous antiviral and anticancer purine nucleoside analog prodrugs. Catalytically active recombinant human GMPK (hGMPK) was purified for the first time and changes in the size and shape of open/closed hGMPK were tracked by SAXS. The binding of substrates (GMP + AMPPNP or Ap5G or GMP + ADP) resulted in the compaction of size and shape of hGMPK. The structural changes between open and completely closed hGMPK conformation were confirmed by observing differences in the hGMPK secondary structures with circular dichroism spectroscopy. [GRAPHICS]"],["dc.description.sponsorship","Max Planck Society; DAAD scholarship; project B10 [SFB 755]"],["dc.identifier.doi","10.1007/s00249-015-1079-9"],["dc.identifier.isi","000367609800009"],["dc.identifier.pmid","26446352"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/12587"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/42115"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.relation.issn","1432-1017"],["dc.relation.issn","0175-7571"],["dc.relation.orgunit","Fakultät für Physik"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.workinggroup","RG Techert (Structural Dynamics in Chemical Systems)"],["dc.rights","CC BY 4.0"],["dc.title","Insights into open/closed conformations of the catalytically active human guanylate kinase as investigated by small-angle X-ray scattering"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]