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The Global ETD Search service is a free service for researchers
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Our metadata is collected from universities around the world. If you manage a university/consortium/country archive and want to be added, details can be found on the NDLTD website.
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Showing 1 to 9 of 9 (0.138 seconds)Spelling suggestions: "subject:"elaxation dispersion"" "subject:"elaxation ispersion""
| 1 |
The Investigation of the pH Effect on Slow Exchange Dynamics in Amino Acids and Proteins with NMR Relaxation Dispersion ExperimentsChen, Yan-wen 09 July 2007 (has links)
None
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| 2 |
The Structure and Unfolding Pathway of γ-Crystallins, and the Solution Structure of a Nucleotide N-glycosidase, RCLMahler, Bryon 23 December 2014 (has links)
No description available.
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| 3 |
A twist in NMR relaxation experiments: Application to the study of protein motionsFrischkorn, Sebastian 04 June 2019 (has links)
No description available.
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| 4 |
Accessing the kinetics of the supra-tauc range via relaxation dispersion NMR spectroscopyBan, David 12 August 2013 (has links)
No description available.
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| 5 |
Cross Validation of the Structure of a Transiently Formed and Low Populated FF Domain Folding Intermediate Determined by Relaxation Dispersion NMR and CS-RosettaBarette, Julia Audrey 01 December 2011 (has links)
The atomic resolution structure of a low populated and transiently formed on-pathway folding intermediate of the FF domain from human HYPA/FBP11 has recently been reported[1]. The structure was determined on the basis of backbone chemical shift and bond vector orientation restraints measured on the ‘invisible’ intermediate state using relaxation dispersion nuclear magnetic resonance (NMR) spectroscopy that were subsequently input into the data-base structure determination program CS-Rosetta. This thesis focuses on the cross-validation of the structure so produced. We present here the solution NMR structure of a mimic of the folding intermediate that is highly populated in solution, obtained from the wild-type domain by protein mutagenesis. The ensemble of structures generated of the mimic are within 2Å of the relaxation dispersion/CS-Rosetta structures of the intermediate, with the non-native interactions in the intermediate also observed in the mimic. The results presented in this thesis strongly confirm the structure of the FF domain folding intermediate, in particular, and validate the use of relaxation dispersion derived restraints in structural studies of invisible excited states, in general.
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| 6 |
Cross Validation of the Structure of a Transiently Formed and Low Populated FF Domain Folding Intermediate Determined by Relaxation Dispersion NMR and CS-RosettaBarette, Julia Audrey 01 December 2011 (has links)
The atomic resolution structure of a low populated and transiently formed on-pathway folding intermediate of the FF domain from human HYPA/FBP11 has recently been reported[1]. The structure was determined on the basis of backbone chemical shift and bond vector orientation restraints measured on the ‘invisible’ intermediate state using relaxation dispersion nuclear magnetic resonance (NMR) spectroscopy that were subsequently input into the data-base structure determination program CS-Rosetta. This thesis focuses on the cross-validation of the structure so produced. We present here the solution NMR structure of a mimic of the folding intermediate that is highly populated in solution, obtained from the wild-type domain by protein mutagenesis. The ensemble of structures generated of the mimic are within 2Å of the relaxation dispersion/CS-Rosetta structures of the intermediate, with the non-native interactions in the intermediate also observed in the mimic. The results presented in this thesis strongly confirm the structure of the FF domain folding intermediate, in particular, and validate the use of relaxation dispersion derived restraints in structural studies of invisible excited states, in general.
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| 7 |
High Resolution Structural and Dynamic Studies of Biomacromolecular Assemblies using Solid-State NMR SpectroscopyShannon, Matthew D. January 2018 (has links)
No description available.
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| 8 |
Approches innovantes en RMN biomoléculaire: Cinétiques moléculaires par RMN rapide et paroi bactérienne par RMN du solideKern, Thomas 22 October 2009 (has links) (PDF)
Les méthodes RMN multidimensionnelles requises pour l'obtention d'une résolution atomique élevée sont relativement couteuses en temps expéri- mental, ce qui complique considérablement leur application à l'analyse d'échantillons en temps réel. La première partie de cette thèse traite des pro- grès récents dans le domaine de l'acquisition rapide des spectres de RMN . La deuxième partie concerne la paroi cellulaire des bactéries Gram-négatives et Gram-positives. En raison de son poids moléculaire élevé et de son car- actère non cristallin, nous avons appliqué la RMN du solide pour l'étudier. La qualité exceptionnelle des spectres de RMN solide permet l'étude, à résolution atomique, de la structure et de la dynamique du peptidoglycane et des acides téchoïques qui se lient de manière covalente au peptidoglycan (WTA). La détermination des propriétés dynamiques du peptidoglycane est aussi utilisée pour étudier les interactions entre protéines et peptidoglycane et la complexation avec des ions divalents.
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| 9 |
Thermodynamic, Kinetic, and Dynamics Studies of the Allosteric Ligand-Responsive Regulatory Protein TRAPKleckner, Ian Robert 19 October 2011 (has links)
No description available.
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