Jain, Rohit

[["dc.bibliographiccitation.artnumber","109"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","The European Physical Journal E - Soft Matter"],["dc.bibliographiccitation.volume","36"],["dc.contributor.author","Jain, R."],["dc.contributor.author","Petri, M."],["dc.contributor.author","Kirschbaum, S."],["dc.contributor.author","Feindt, H."],["dc.contributor.author","Steltenkamp, Siegfried"],["dc.contributor.author","Sonnenkalb, S."],["dc.contributor.author","Becker, S."],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Menzel, A."],["dc.contributor.author","Burg, T. P."],["dc.contributor.author","Techert, S."],["dc.date.accessioned","2017-09-07T11:47:08Z"],["dc.date.available","2017-09-07T11:47:08Z"],["dc.date.issued","2013"],["dc.description.abstract","Small-angle X-ray scattering provides global, shape-sensitive structural information about macromolecules in solution. Its extension to time dimension in the form of time-resolved SAXS investigations and combination with other time-resolved biophysical methods contributes immensely to the study of protein dynamics. TR-SAXS can also provide unique information about the global structures of transient intermediates during protein dynamics. An experimental set-up with low protein consumption is essential for an extensive use of TR-SAXS experiments on protein dynamics. In this direction, a newly developed 20-microchannel microfluidic continuous-flow mixer was combined with SAXS. With this set-up, we demonstrate ubiquitin unfolding dynamics after rapid mixing with the chaotropic agent Guanidinium-HCl within milliseconds using only similar to 40 nanoliters of the protein sample per scattering image. It is suggested that, in the future, this new TR-SAXS platform will help to increase the use of time-resolved small-angle X-ray scattering, wide-angle X-ray scattering and neutron scattering experiments for studying protein dynamics in the early millisecond regime. The potential research field for this set-up includes protein folding, protein misfolding, aggregation in amyloidogenic diseases, function of intrinsically disordered proteins and various protein-ligand interactions."],["dc.identifier.doi","10.1140/epje/i2013-13109-9"],["dc.identifier.gro","3142281"],["dc.identifier.isi","000325224100001"],["dc.identifier.pmid","24092048"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/6542"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: Nanoscale Photon Imaging of the DFG [SFB 755]"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","1292-8941"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.workinggroup","RG Techert (Structural Dynamics in Chemical Systems)"],["dc.title","X-ray scattering experiments with high-flux X-ray source coupled rapid mixing microchannel device and their potential for high-flux neutron scattering investigations"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","242"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Protein and Peptide Letters"],["dc.bibliographiccitation.lastpage","254"],["dc.bibliographiccitation.volume","23"],["dc.contributor.author","Jain, Rohit"],["dc.contributor.author","Techert, Simone"],["dc.date.accessioned","2018-11-07T10:20:39Z"],["dc.date.available","2018-11-07T10:20:39Z"],["dc.date.issued","2016"],["dc.description.abstract","X-ray scattering technique, comprising of small-angle/wide-angle X-ray scattering (SAXS/WAXS) techniques is increasingly used to characterize the structure and interactions of biological macromolecules and their complexes in solution. It is a method of choice to characterize the flexible, partially folded and unfolded protein systems. X-ray scattering is the last resort for proteins that cannot be investigated by crystallography or NMR and acts as a complementary technique with different biophysical techniques to answer challenging scientific questions. The marriage of the X-ray scattering technique with the fourth dimension \"time\" yields structural dynamics and kinetics information for protein motions in hierarchical timescales from picoseconds to days. The arrival of the high-flux X-ray beam at third generation synchrotron sources, exceptional X-ray optics, state-of-the-art detectors, upgradation of X-ray scattering beamlines with microfluidics devices and advanced X-ray scattering data analysis procedures are the important reasons behind the shining years of X-ray scattering technique. The best days of the X-ray scattering technique are on the horizon with the advent of the nanofocus X-ray scattering beamlines and fourth generation X-ray lightsources, i.e., free electron lasers (XFELs). Complementary to the photon-triggered time-resolved X-ray scattering techniques, we will present an overview of the time-resolved and in-situ X-ray scattering techniques for structural dynamics of ubiquitous non-photoactive proteins."],["dc.description.sponsorship","Helmholtz Society; Max Planck Society; [SFB 755]"],["dc.identifier.doi","10.2174/0929866523666160106153847"],["dc.identifier.isi","000373714100006"],["dc.identifier.pmid","26732244"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/41930"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.relation.issn","1875-5305"],["dc.relation.issn","0929-8665"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.workinggroup","RG Techert (Structural Dynamics in Chemical Systems)"],["dc.title","Time-Resolved and In-Situ X-Ray Scattering Methods Beyond Photoactivation: Utilizing High-Flux X-Ray Sources for the Study of Ubiquitous Non-Photoactive Proteins"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","184904"],["dc.bibliographiccitation.issue","18"],["dc.bibliographiccitation.journal","The Journal of Chemical Physics"],["dc.bibliographiccitation.volume","154"],["dc.contributor.author","Jain, Rohit"],["dc.contributor.author","Ginot, Félix"],["dc.contributor.author","Berner, Johannes"],["dc.contributor.author","Bechinger, Clemens"],["dc.contributor.author","Krüger, Matthias"],["dc.date.accessioned","2021-10-01T09:57:51Z"],["dc.date.available","2021-10-01T09:57:51Z"],["dc.date.issued","2021"],["dc.identifier.doi","10.1063/5.0048320"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/89928"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-469"],["dc.relation.eissn","1089-7690"],["dc.relation.issn","0021-9606"],["dc.title","Two step micro-rheological behavior in a viscoelastic fluid"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","103101"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Physics of Fluids"],["dc.bibliographiccitation.volume","33"],["dc.contributor.author","Jain, Rohit"],["dc.contributor.author","Ginot, Félix"],["dc.contributor.author","Krüger, Matthias"],["dc.date.accessioned","2022-02-01T10:31:16Z"],["dc.date.available","2022-02-01T10:31:16Z"],["dc.date.issued","2021"],["dc.identifier.doi","10.1063/5.0062104"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/98815"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-517"],["dc.relation.eissn","1089-7666"],["dc.relation.issn","1070-6631"],["dc.title","Micro-rheology of a particle in a nonlinear bath: Stochastic Prandtl–Tomlinson model"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["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"]]