Reddy, Jithender G.

[["dc.bibliographiccitation.firstpage","1"],["dc.bibliographiccitation.journal","Journal of Biomolecular NMR"],["dc.bibliographiccitation.lastpage","9"],["dc.contributor.author","Reddy, Jithender G."],["dc.contributor.author","Pratihar, Supriya"],["dc.contributor.author","Frischkorn, Sebastian"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Lee, Donghan"],["dc.date.accessioned","2018-01-17T11:30:39Z"],["dc.date.available","2018-01-17T11:30:39Z"],["dc.date.issued","2017"],["dc.description.abstract","Molecular dynamics play a significant role in how molecules perform their function. A critical method that provides information on dynamics, at the atomic level, is NMR-based relaxation dispersion (RD) experiments. RD experiments have been utilized for understanding multiple biological processes occurring at micro-to-millisecond time, such as enzyme catalysis, molecular recognition, ligand binding and protein folding. Here, we applied the recently developed high-power RD concept to the Carr-Purcell-Meiboom-Gill sequence (extreme CPMG; E-CPMG) for the simultaneous detection of fast and slow dynamics. Using a fast folding protein, gpW, we have shown that previously inaccessible kinetics can be accessed with the improved precision and efficiency of the measurement by using this experiment."],["dc.identifier.doi","10.1007/s10858-017-0155-0"],["dc.identifier.pmid","29188417"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/11678"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.relation.eissn","1573-5001"],["dc.title","Simultaneous determination of fast and slow dynamics in molecules using extreme CPMG relaxation dispersion experiments"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","65"],["dc.bibliographiccitation.journal","Journal of Magnetic Resonance (1969)"],["dc.bibliographiccitation.lastpage","69"],["dc.bibliographiccitation.volume","269"],["dc.contributor.author","Chakrabarti, Kalyan S."],["dc.contributor.author","Ban, David"],["dc.contributor.author","Pratihar, Supriya"],["dc.contributor.author","Reddy, Jithender G."],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Lee, Donghan"],["dc.date.accessioned","2017-09-07T11:44:45Z"],["dc.date.available","2017-09-07T11:44:45Z"],["dc.date.issued","2016"],["dc.description.abstract","Exchange-mediated saturation transfer (EST) provides critical information regarding dynamics of molecules. In typical applications EST is studied by either scanning a wide range of N-15 chemical shift offsets where the applied N-15 irradiation field strength is on the order of hundreds of Hertz or, scanning a narrow range of N-15 chemical shift offsets where the applied N-15 irradiation field-strength is on the order of tens of Hertz during the EST period. The H-1 decoupling during the EST delay is critical as incomplete decoupling causes broadening of the EST profile, which could possibly result in inaccuracies of the extracted kinetic parameters and transverse relaxation rates. Currently two different H-1 decoupling schemes have been employed, intermittently applied 180 pulses and composite-pulse-decoupling (CPD), for situations where a wide range, or narrow range of N-15 chemical shift offsets are scanned, respectively. We show that high-power CPD provides artifact free EST experiments, which can be universally implemented regardless of the offset range or irradiation field-strengths. (C) 2016 Elsevier Inc. All rights reserved."],["dc.identifier.doi","10.1016/j.jmr.2016.05.013"],["dc.identifier.gro","3141641"],["dc.identifier.isi","000381239900007"],["dc.identifier.pmid","27240144"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/4344"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: Max Planck Society; EU (ERC) [233227]; James Graham Brown Foundation"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Academic Press Inc Elsevier Science"],["dc.relation.eissn","1096-0856"],["dc.relation.issn","1090-7807"],["dc.title","High-power H-1 composite pulse decoupling provides artifact free exchange-mediated saturation transfer (EST) experiments"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","6503"],["dc.bibliographiccitation.issue","26"],["dc.bibliographiccitation.journal","Chemical Science"],["dc.bibliographiccitation.lastpage","6507"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Ambadipudi, Susmitha"],["dc.contributor.author","Reddy, Jithender G."],["dc.contributor.author","Biernat, Jacek"],["dc.contributor.author","Mandelkow, Eckhard"],["dc.contributor.author","Zweckstetter, Markus"],["dc.date.accessioned","2019-09-30T09:26:49Z"],["dc.date.accessioned","2021-10-27T13:21:20Z"],["dc.date.available","2019-09-30T09:26:49Z"],["dc.date.available","2021-10-27T13:21:20Z"],["dc.date.issued","2019"],["dc.description.abstract","Liquid-liquid phase separation (LLPS) of proteins enables the formation of non-membrane-bound organelles in cells and is associated with cancer and neurodegeneration. Little is known however about the structure and dynamics of proteins in LLPS conditions, because of the polymorphic nature of liquid-like protein droplets. Using carbon-detected NMR experiments we here show that the conversion of the aggregation-prone repeat region of the Alzheimer's-related protein tau from the dispersed monomeric state to phase-separated liquid-like droplets involves tau's aggregation-prone hexapeptides and regulatory KXGS motifs. Droplet dissolution in presence of 1,6-hexanediol revealed that chemical shift perturbations in the hexapeptide motifs are temperature driven, while those in KXGS motifs report on phase separation. Residue-specific secondary structure analysis further indicated that tau's repeat region exists in extended conformation in the dispersed state and attains transient β-hairpin propensity upon LLPS. Taken together our work shows that NMR spectroscopy can provide high-resolution insights into LLPS-induced changes in intrinsically disordered proteins."],["dc.identifier.doi","10.1039/C9SC00531E"],["dc.identifier.pmid","31341602"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16419"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/92013"],["dc.language.iso","en"],["dc.notes.intern","Migrated from goescholar"],["dc.relation.eissn","2041-6539"],["dc.relation.issn","2041-6520"],["dc.relation.orgunit","Universitätsmedizin Göttingen"],["dc.rights","CC BY-NC 3.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc/3.0"],["dc.subject.ddc","610"],["dc.title","Residue-specific identification of phase separation hot spots of Alzheimer's-related protein tau"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","237"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Journal of Biomolecular NMR"],["dc.bibliographiccitation.lastpage","244"],["dc.bibliographiccitation.volume","63"],["dc.contributor.author","Carneiro, Marta G."],["dc.contributor.author","Reddy, Jithender G."],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Lee, Donghan"],["dc.date.accessioned","2017-09-07T11:43:27Z"],["dc.date.available","2017-09-07T11:43:27Z"],["dc.date.issued","2015"],["dc.description.abstract","Protein motions over various time scales are crucial for protein function. NMR relaxation dispersion experiments play a key role in explaining these motions. However, the study of slow conformational changes with lowly populated states remained elusive. The recently developed exchange-mediated saturation transfer experiments allow the detection and characterization of such motions, but require extensive measurement time. Here we show that, by making use of Fourier transform, the total acquisition time required to measure an exchange-mediated saturation transfer profile can be reduced by twofold in case that one applies linear prediction. In addition, we demonstrate that the analytical solution for R-1 rho experiments can be used for fitting the exchange-mediated saturation transfer profile. Furthermore, we show that simultaneous analysis of exchange-mediated saturation transfer profiles with two different radio-frequency field strengths is required for accurate and precise characterization of the exchange process and the exchanging states."],["dc.identifier.doi","10.1007/s10858-015-9985-9"],["dc.identifier.gro","3141796"],["dc.identifier.isi","000365088800001"],["dc.identifier.pmid","26350257"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1168"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: James Graham Brown Foundation; Max Planck Society; EU (ERC) [233227]"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1573-5001"],["dc.relation.issn","0925-2738"],["dc.title","Speeding-up exchange-mediated saturation transfer experiments by Fourier transform"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]