Sabo, Thomas Michael

[["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","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"]]

[["dc.bibliographiccitation.firstpage","9566"],["dc.bibliographiccitation.issue","33"],["dc.bibliographiccitation.journal","Angewandte Chemie International Edition"],["dc.bibliographiccitation.lastpage","9569"],["dc.bibliographiccitation.volume","55"],["dc.contributor.author","Pratihar, Supriya"],["dc.contributor.author","Sabo, T. Michael"],["dc.contributor.author","Ban, David"],["dc.contributor.author","Fenwick, R. Bryn"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Salvatella, Xavier"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Lee, Donghan"],["dc.date.accessioned","2017-09-07T11:44:44Z"],["dc.date.available","2017-09-07T11:44:44Z"],["dc.date.issued","2016"],["dc.description.abstract","Protein dynamics occurring on a wide range of timescales play a crucial role in governing protein function. Particularly, motions between the globular rotational correlation time (tau(c)) and 40 mu s (supra-tau(c) window), strongly influence molecular recognition. This supra-tau(c) window was previously hidden, owing to a lack of experimental methods. Recently, we have developed a high-power relaxation dispersion (RD) experiment for measuring kinetics as fast as 4 mu s. For the first time, this method, performed under super-cooled conditions, enabled us to detect a global motion in the first mu beta-turn of the third IgG-binding domain of protein G (GB3), which was extrapolated to 371 +/- 115 ns at 310 K. Furthermore, the same residues show the plasticity in the model-free residual dipolar coupling (RDC) order parameters and in an ensemble encoding the supra-tau(c) dynamics. This beta-turn is involved in antibody binding, exhibiting the potential link of the observed supra-tau(c) motion with molecular recognition."],["dc.identifier.doi","10.1002/anie.201603501"],["dc.identifier.gro","3141635"],["dc.identifier.isi","000383372700016"],["dc.identifier.pmid","27345359"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/3678"],["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","1521-3773"],["dc.relation.issn","1433-7851"],["dc.title","Kinetics of the Antibody Recognition Site in the Third IgG-Binding Domain of Protein G"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","73"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Journal of Biomolecular NMR"],["dc.bibliographiccitation.lastpage","82"],["dc.bibliographiccitation.volume","57"],["dc.contributor.author","Ban, David"],["dc.contributor.author","Mazur, Adam"],["dc.contributor.author","Carneiro, Marta G."],["dc.contributor.author","Sabo, T. Michael"],["dc.contributor.author","Giller, Karin"],["dc.contributor.author","Koharudin, Leonardus M. I."],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Gronenborn, Angela M."],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Lee, Donghan"],["dc.date.accessioned","2017-09-07T11:47:37Z"],["dc.date.available","2017-09-07T11:47:37Z"],["dc.date.issued","2013"],["dc.description.abstract","Micro-to-millisecond motions of proteins transmit pivotal signals for protein function. A powerful technique for the measurement of these motions is nuclear magnetic resonance spectroscopy. One of the most widely used methodologies for this purpose is the constant-time Carr-Purcell-Meiboom-Gill (CT-CPMG) relaxation dispersion experiment where kinetic and structural information can be obtained at atomic resolution. Extraction of accurate kinetics determined from CT-CPMG data requires refocusing frequencies that are much larger than the nuclei's exchange rate between states. We investigated the effect when fast processes are probed by CT-CPMG experiments via simulation and show that if the intrinsic relaxation rate is not known a priori the extraction of accurate kinetics is hindered. Errors on the order of 50 % in the exchange rate are attained when processes become fast, but are minimized to 5 % with a priori information. To alleviate this shortcoming, we developed an experimental scheme probing with large amplitude spin-lock fields, which specifically contains the intrinsic proton longitudinal Eigenrelaxation rate. Our approach was validated with ubiquitin and the Oscillatoria agardhii agglutinin (OAA). For OAA, an underestimation of 66 % in the kinetic rates was observed if is not included during the analysis of CT-CPMG data and result in incorrect kinetics and imprecise amplitude information. This was overcome by combining CT-CPMG with measured with a high power R-1 rho experiment. In addition, the measurement of removes the ambiguities in choosing between different models that describe CT-CPMG data."],["dc.identifier.doi","10.1007/s10858-013-9769-z"],["dc.identifier.gro","3142293"],["dc.identifier.isi","000323673800009"],["dc.identifier.pmid","23949308"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/6676"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: Max Planck Society; EU (ERC) [233227]; NIH [GM080642]"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Springer"],["dc.relation.issn","0925-2738"],["dc.title","Enhanced accuracy of kinetic information from CT-CPMG experiments by transverse rotating-frame spectroscopy"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","85"],["dc.bibliographiccitation.journal","Methods"],["dc.bibliographiccitation.lastpage","92"],["dc.bibliographiccitation.volume","138-139"],["dc.contributor.author","Sabo, T. Michael"],["dc.contributor.author","Gapsys, Vytautas"],["dc.contributor.author","Walter, Korvin F. A."],["dc.contributor.author","Fenwick, R. Bryn"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Salvatella, Xavier"],["dc.contributor.author","de Groot, Bert L."],["dc.contributor.author","Lee, Donghan"],["dc.contributor.author","Griesinger, Christian"],["dc.date.accessioned","2021-03-05T08:58:13Z"],["dc.date.available","2021-03-05T08:58:13Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.1016/j.ymeth.2018.04.007"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/80045"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-393"],["dc.relation.issn","1046-2023"],["dc.title","Utilizing dipole-dipole cross-correlated relaxation for the measurement of angles between pairs of opposing CαHα-CαHα bonds in anti-parallel β-sheets"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","439a"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.volume","106"],["dc.contributor.author","Michielssens, Servaas"],["dc.contributor.author","Peters, Jan Henning"],["dc.contributor.author","Ban, David"],["dc.contributor.author","Pratihar, Supriya"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Sabo, Thomas Michael"],["dc.contributor.author","Giller, Karin"],["dc.contributor.author","Lee, Donghan"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","de Groot, Bert L."],["dc.date.accessioned","2021-03-05T08:57:57Z"],["dc.date.available","2021-03-05T08:57:57Z"],["dc.date.issued","2014"],["dc.identifier.doi","10.1016/j.bpj.2013.11.2471"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/79942"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-393"],["dc.relation.issn","0006-3495"],["dc.title","Controlling Protein Binding Specificity by a Conformational Shift"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","11437"],["dc.bibliographiccitation.issue","48"],["dc.bibliographiccitation.journal","Angewandte Chemie International Edition"],["dc.bibliographiccitation.lastpage","11440"],["dc.bibliographiccitation.volume","50"],["dc.contributor.author","Ban, David"],["dc.contributor.author","Funk, Michael"],["dc.contributor.author","Gulich, Rudolf"],["dc.contributor.author","Egger, Dalia"],["dc.contributor.author","Sabo, T. Michael"],["dc.contributor.author","Walter, Korvin F. A."],["dc.contributor.author","Fenwick, R. Bryn"],["dc.contributor.author","Giller, Karin"],["dc.contributor.author","Pichierri, Fabio"],["dc.contributor.author","Groot, Bert L. de"],["dc.contributor.author","Lange, Oliver F."],["dc.contributor.author","Grubmüller, Helmut"],["dc.contributor.author","Salvatella, Xavier"],["dc.contributor.author","Wolf, Martin"],["dc.contributor.author","Loidl, Alois"],["dc.contributor.author","Kree, Reiner"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Lakomek, Nils-Alexander"],["dc.contributor.author","Lee, Donghan"],["dc.contributor.author","Lunkenheimer, Peter"],["dc.contributor.author","Griesinger, Christian"],["dc.date.accessioned","2017-09-07T11:45:04Z"],["dc.date.available","2017-09-07T11:45:04Z"],["dc.date.issued","2011"],["dc.description.abstract","The lifetime of interconversion among the ground states of a protein ensemble representation could only be assigned to a time window that is four orders of magnitude large and ranges from 4 ns to 50 μs. By combining temperature-dependent NMR relaxation dispersion (RD) experiments and dielectric relaxation (DR) spectroscopy in solution, the lifetime was now identified to a value of (10±9) μs at 309 K."],["dc.identifier.doi","10.1002/anie.201105086"],["dc.identifier.gro","3142794"],["dc.identifier.isi","000297863900026"],["dc.identifier.pmid","22113802"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/238"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","1433-7851"],["dc.title","Kinetics of Conformational Sampling in Ubiquitin"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]