Griesinger, Christian

[["dc.bibliographiccitation.firstpage","81"],["dc.bibliographiccitation.journal","Archives of Biochemistry and Biophysics"],["dc.bibliographiccitation.lastpage","91"],["dc.bibliographiccitation.volume","628"],["dc.contributor.author","Ban, David"],["dc.contributor.author","Smith, Colin A."],["dc.contributor.author","de Groot, Bert L."],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Lee, Donghan"],["dc.date.accessioned","2018-01-17T11:31:26Z"],["dc.date.available","2018-01-17T11:31:26Z"],["dc.date.issued","2017"],["dc.description.abstract","Protein function can be modulated or dictated by the amplitude and timescale of biomolecular motion, therefore it is imperative to study protein dynamics. Nuclear Magnetic Resonance (NMR) spectroscopy is a powerful technique capable of studying timescales of motion that range from those faster than molecular reorientation on the picosecond timescale to those that occur in real-time. Across this entire regime, NMR observables can report on the amplitude of atomic motion, and the kinetics of atomic motion can be ascertained with a wide variety of experimental techniques from real-time to milliseconds and several nanoseconds to picoseconds. Still a four orders of magnitude window between several nanoseconds and tens of microseconds has remained elusive. Here, we highlight new relaxation dispersion NMR techniques that serve to cover this \"hidden-time\" window up to hundreds of nanoseconds that achieve atomic resolution while studying the molecule under physiological conditions."],["dc.identifier.doi","10.1016/j.abb.2017.05.016"],["dc.identifier.pmid","28576576"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/11679"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.relation.eissn","1096-0384"],["dc.title","Recent advances in measuring the kinetics of biomolecules by NMR relaxation dispersion spectroscopy"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","8971"],["dc.bibliographiccitation.issue","47"],["dc.bibliographiccitation.journal","Angewandte Chemie International Edition"],["dc.bibliographiccitation.lastpage","8974"],["dc.bibliographiccitation.volume","49"],["dc.contributor.author","Himmel, Sebastian"],["dc.contributor.author","Wolff, Sebastian"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Lee, Donghan"],["dc.contributor.author","Griesinger, Christian"],["dc.date.accessioned","2017-09-07T11:46:11Z"],["dc.date.available","2017-09-07T11:46:11Z"],["dc.date.issued","2010"],["dc.identifier.doi","10.1002/anie.201003965"],["dc.identifier.gro","3142990"],["dc.identifier.isi","000284708400014"],["dc.identifier.pmid","20939030"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/454"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: Max-Planck Gesellschaft"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Wiley-v C H Verlag Gmbh"],["dc.relation.issn","1433-7851"],["dc.title","Detection and Identification of Protein-Phosphorylation Sites in Histidines through HNP Correlation Patterns"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","27731"],["dc.bibliographiccitation.issue","33"],["dc.bibliographiccitation.journal","Journal of biological chemistry"],["dc.bibliographiccitation.lastpage","27742"],["dc.bibliographiccitation.volume","287"],["dc.contributor.author","Himmel, Sebastian"],["dc.contributor.author","Zschiedrich, Christopher P."],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Hsiao, He-Hsuan"],["dc.contributor.author","Wolff, Sebastian"],["dc.contributor.author","Diethmaier, Christine"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Lee, Donghan"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Stuelke, Joerg"],["dc.date.accessioned","2017-09-07T11:48:29Z"],["dc.date.available","2017-09-07T11:48:29Z"],["dc.date.issued","2012"],["dc.description.abstract","The control of several catabolic operons in bacteria by transcription antitermination is mediated by RNA-binding proteins that consist of an RNA-binding domain and two reiterated phosphotransferase system regulation domains (PRDs). The Bacillus subtilis GlcT antitermination protein regulates the expression of the ptsG gene, encoding the glucose-specific enzyme II of the phosphotransferase system. In the absence of glucose, GlcT becomes inactivated by enzyme II-dependent phosphorylation at its PRD1, whereas the phosphotransferase HPr phosphorylates PRD2. However, here we demonstrate by NMR analysis and mass spectrometry that HPr also phosphorylates PRD1 in vitro but with low efficiency. Size exclusion chromatography revealed that non-phosphorylated PRD1 forms dimers that dissociate upon phosphorylation. The effect of HPr on PRD1 was also investigated in vivo. For this purpose, we used GlcT variants with altered domain arrangements or domain deletions. Our results demonstrate that HPr can target PRD1 when this domain is placed at the C terminus of the protein. In agreement with the in vitro data, HPr exerts a negative control on PRD1. This work provides the first insights into how specificity is achieved in a regulator that contains duplicated regulatory domains with distinct dimerization properties that are controlled by phosphorylation by different phosphate donors. Moreover, the results suggest that the domain arrangement of the PRD-containing antitermination proteins is under selective pressure to ensure the proper regulatory output, i.e. transcription antitermination of the target genes specifically in the presence of the corresponding sugar."],["dc.identifier.doi","10.1074/jbc.M112.388850"],["dc.identifier.gro","3142483"],["dc.identifier.isi","000307840700047"],["dc.identifier.pmid","22722928"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8785"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Amer Soc Biochemistry Molecular Biology Inc"],["dc.relation.issn","0021-9258"],["dc.title","Determinants of Interaction Specificity of the Bacillus subtilis GlcT Antitermination Protein FUNCTIONALITY AND PHOSPHORYLATION SPECIFICITY DEPEND ON THE ARRANGEMENT OF THE REGULATORY DOMAINS"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","680"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","EMBO Journal"],["dc.bibliographiccitation.lastpage","691"],["dc.bibliographiccitation.volume","29"],["dc.contributor.author","Rodriguez-Castaneda, Fernando"],["dc.contributor.author","Maestre-Martinez, Mitcheell"],["dc.contributor.author","Coudevylle, Nicolas"],["dc.contributor.author","Dimova, Kalina"],["dc.contributor.author","Junge, Harald J."],["dc.contributor.author","Lipstein, Noa"],["dc.contributor.author","Lee, Donghan"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Brose, Nils"],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Carlomagno, Teresa"],["dc.contributor.author","Griesinger, Christian"],["dc.date.accessioned","2017-09-07T11:46:08Z"],["dc.date.available","2017-09-07T11:46:08Z"],["dc.date.issued","2010"],["dc.description.abstract","Ca²⁺ signalling in neurons through calmodulin (CaM) has a prominent function in regulating synaptic vesicle trafficking, transport, and fusion. Importantly, Ca²⁺–CaM binds a conserved region in the priming proteins Munc13‐1 and ubMunc13‐2 and thus regulates synaptic neurotransmitter release in neurons in response to residual Ca2+ signals. We solved the structure of Ca²⁺₄–CaM in complex with the CaM‐binding domain of Munc13‐1, which features a novel 1‐5‐8‐26 CaM‐binding motif with two separated mobile structural modules, each involving a CaM domain. Photoaffinity labelling data reveal the same modular architecture in the complex with the ubMunc13‐2 isoform. The N‐module can be dissociated with EGTA to form the half‐loaded Munc13/Ca²⁺₂–CaM complex. The Ca²⁺ regulation of these Munc13 isoforms can therefore be explained by the modular nature of the Munc13/Ca²⁺–CaM interactions, where the C‐module provides a high‐affinity interaction activated at nanomolar [Ca²⁺]i, whereas the N‐module acts as a sensor at micromolar [Ca²⁺]i. This Ca²⁺/CaM‐binding mode of Munc13 likely constitutes a key molecular correlate of the characteristic Ca²⁺‐dependent modulation of short‐term synaptic plasticity."],["dc.identifier.doi","10.1038/emboj.2009.373"],["dc.identifier.gro","3142967"],["dc.identifier.isi","000274233400015"],["dc.identifier.pmid","20010694"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/429"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: Max-Planck Society; Fonds der Chemischen Industrie"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","0261-4189"],["dc.title","Modular architecture of Munc13/calmodulin complexes: dual regulation by Ca²⁺ and possible function in short-term synaptic plasticity"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["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","1819"],["dc.bibliographiccitation.issue","14"],["dc.bibliographiccitation.journal","Bioinformatics"],["dc.bibliographiccitation.lastpage","1820"],["dc.bibliographiccitation.volume","29"],["dc.contributor.author","Mazur, Adam"],["dc.contributor.author","Hammesfahr, Björn"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Lee, Donghan"],["dc.contributor.author","Kollmar, Martin"],["dc.date.accessioned","2017-09-07T11:47:39Z"],["dc.date.available","2017-09-07T11:47:39Z"],["dc.date.issued","2013"],["dc.description.abstract","Dynamics governing the function of biomolecule is usually described as exchange processes and can be monitored at atomic resolution with nuclear magnetic resonance (NMR) relaxation dispersion data. Here, we present a new tool for the analysis of CPMG relaxation dispersion profiles (ShereKhan). The web interface to ShereKhan provides a user-friendly environment for the analysis."],["dc.identifier.doi","10.1093/bioinformatics/btt286"],["dc.identifier.gro","3142323"],["dc.identifier.isi","000321747800020"],["dc.identifier.pmid","23698862"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/7009"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Oxford Univ Press"],["dc.relation.issn","1367-4803"],["dc.title","ShereKhan-calculating exchange parameters in relaxation dispersion data from CPMG experiments"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","10367"],["dc.bibliographiccitation.issue","39"],["dc.bibliographiccitation.journal","Angewandte Chemie International Edition"],["dc.bibliographiccitation.lastpage","10371"],["dc.bibliographiccitation.volume","53"],["dc.contributor.author","Michielssens, Servaas"],["dc.contributor.author","Peters, Jan Henning"],["dc.contributor.author","Ban, David"],["dc.contributor.author","Pratihar, Supriya"],["dc.contributor.author","Seeliger, Daniel"],["dc.contributor.author","Sharma, Monika"],["dc.contributor.author","Giller, Karin"],["dc.contributor.author","Sabo, Thomas Michael"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Lee, Donghan"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Groot, Bert L. de"],["dc.date.accessioned","2017-09-07T11:45:30Z"],["dc.date.available","2017-09-07T11:45:30Z"],["dc.date.issued","2014"],["dc.description.abstract","In a conformational selection scenario, manipulating the populations of binding-competent states should be expected to affect protein binding. We demonstrate how in silico designed point mutations within the core of ubiquitin, remote from the binding interface, change the binding specificity by shifting the conformational equilibrium of the ground-state ensemble between open and closed substates that have a similar population in the wild-type protein. Binding affinities determined by NMR titration experiments agree with the predictions, thereby showing that, indeed, a shift in the conformational equilibrium enables us to alter ubiquitin's binding specificity and hence its function. Thus, we present a novel route towards designing specific binding by a conformational shift through exploiting the fact that conformational selection depends on the concentration of binding-competent substates."],["dc.identifier.doi","10.1002/anie.201403102"],["dc.identifier.gro","3142049"],["dc.identifier.isi","000342760700013"],["dc.identifier.pmid","25115701"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/3978"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1521-3773"],["dc.relation.issn","1433-7851"],["dc.title","A Designed Conformational Shift To Control Protein Binding Specificity"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","366"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Molecular BioSystems"],["dc.bibliographiccitation.lastpage","369"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Kim, Do-Hyoung"],["dc.contributor.author","Lee, Chewook"],["dc.contributor.author","Cho, Ye-Jin"],["dc.contributor.author","Lee, Si-Hyung"],["dc.contributor.author","Cha, Eun-Ji"],["dc.contributor.author","Lim, Ji-Eun"],["dc.contributor.author","Sabo, T. Michael"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Lee, Donghan"],["dc.contributor.author","Han, Kyou-Hoon"],["dc.date.accessioned","2017-09-07T11:44:46Z"],["dc.date.available","2017-09-07T11:44:46Z"],["dc.date.issued","2015"],["dc.description.abstract","The eIF4E-binding protein 1 (4EBP1) has long been known to be completely unstructured without any secondary structures, which contributed significantly to the proposal of the induced fit mechanism for target binding of intrinsically disordered proteins. We show here that 4EBP1 is not completely unstructured, but contains a pre-structured helix."],["dc.identifier.doi","10.1039/c4mb00532e"],["dc.identifier.gro","3141987"],["dc.identifier.isi","000348211900005"],["dc.identifier.pmid","25431930"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/3290"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1742-2051"],["dc.relation.issn","1742-206X"],["dc.title","A pre-structured helix in the intrinsically disordered 4EBP1"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","184a"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.lastpage","185a"],["dc.bibliographiccitation.volume","108"],["dc.contributor.author","Smith, Colin A."],["dc.contributor.author","Ban, David"],["dc.contributor.author","Giller, Karin"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Lee, Donghan"],["dc.contributor.author","Groot, Bert L. de"],["dc.date.accessioned","2017-09-07T11:52:26Z"],["dc.date.available","2017-09-07T11:52:26Z"],["dc.date.issued","2015"],["dc.description.abstract","Motion is involved in a large number of protein functions. Relaxation dispersion (RD) NMR experiments sensitively probe microsecond to millisecond motions. We conducted an in-depth RD analysis of the backbone and side chain methyl groups of ubquitin. This survey showed a large number of atoms (>30) with microsecond fluctuations. These atoms are distributed throughout the structure. Strikingly, nearly all show the same exchange rate, which suggests that ubiquitin undergoes collective motion involving both the backbone and side chains. Furthermore, comparison of different methyl nuclei indicates that the nature of the side chain fluctuations is almost entirely due to changes in rotamer populations. Thus, collective microsecond backbone motion is coupled to redistribution of side chain rotamer populations through a mechanism we term “population shuffling”. We present a single collective mode of motion that yields a reaction coordinate corresponding to the relaxation dispersion data. The resulting model indicates that a localized conformational switch distant from the binding interface propagates changes throughout the structure. Analysis of crystal structures confirms this allosteric network and suggests that the microsecond motion modulates binding to particular interaction partners."],["dc.identifier.doi","10.1016/j.bpj.2014.11.1020"],["dc.identifier.gro","3144936"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/2615"],["dc.language.iso","en"],["dc.notes.intern","Crossref Import"],["dc.notes.status","final"],["dc.relation.issn","0006-3495"],["dc.title","Microsecond Motion Modulates Ubiquitin Binding through an Allosteric Backbone/Side Chain Network"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","562"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Protein Science"],["dc.bibliographiccitation.lastpage","570"],["dc.bibliographiccitation.volume","21"],["dc.contributor.author","Sabo, T. Michael"],["dc.contributor.author","Bakhtiari, Davood"],["dc.contributor.author","Walter, Korvin F. A."],["dc.contributor.author","McFeeters, Robert L."],["dc.contributor.author","Giller, Karin"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Lee, Donghan"],["dc.date.accessioned","2017-09-07T11:48:55Z"],["dc.date.available","2017-09-07T11:48:55Z"],["dc.date.issued","2012"],["dc.description.abstract","Physiological processes such as protein folding and molecular recognition are intricately linked to their dynamic signature, which is reflected in their thermal coefficient. In addition, the local conformational entropy is directly related to the degrees of freedom, which each residue possesses within its conformational space. Therefore, the temperature dependence of the local conformational entropy may provide insight into understanding how local dynamics may affect the stability of proteins. Here, we analyze the temperature dependence of internal methyl group dynamics derived from the cross-correlated relaxation between dipolar couplings of two CH bonds within ubiquitin. Spanning a temperature range from 275 to 308 K, internal methyl group dynamics tend to increase with increasing temperature, which translates to a general increase in local conformational entropy. With this data measured over multiple temperatures, the thermal coefficient of the methyl group order parameter, the characteristic thermal coefficient, and the local heat capacity were obtained. By analyzing the distribution of methyl group thermal coefficients within ubiquitin, we found that the N-terminal region has relatively high thermostability. These results indicate that methyl groups contribute quite appreciably to the total heat capacity of ubiquitin through the regulation of local conformational entropy."],["dc.identifier.doi","10.1002/pro.2045"],["dc.identifier.gro","3142558"],["dc.identifier.isi","000301576100012"],["dc.identifier.pmid","22334336"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8922"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Wiley-blackwell"],["dc.relation.issn","0961-8368"],["dc.title","Thermal coefficients of the methyl groups within ubiquitin"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]