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The development of methods to study structure and dynamics in biological systems using solid-state NMR
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Tatman, Ben P. (2023) The development of methods to study structure and dynamics in biological systems using solid-state NMR. PhD thesis, University of Warwick.
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WRAP_Theses_Tatman_2023.pdf - Submitted Version - Requires a PDF viewer. Download (37Mb) | Preview |
Official URL: http://webcat.warwick.ac.uk/record=b3986027
Abstract
Solid-state Nuclear Magnetic Resonance (NMR) can provide insight into the structure and dynamics of biological systems. Magic-Angle Spinning (MAS) can help to increase the limited resolution and sensitivity of the technique. This thesis aims to both investigate how fast MAS may affect spin diffusion and to develop methodology to enable greater insight into the local molecular motions occurring in protein systems.
Under fast MAS conditions, the coherent diffusion of spin order becomes strongly dependent on resonance offset. In Chapter 4, a new basis set selection method is introduced to enable the application of low-order Liouville space methods to the simulation of spin diffusion under fast MAS conditions. Consideration is given to the effects of spinning frequency, magnetic field, and dynamics. In Section 4.5, two experimental case studies are introduced to explore the experimental impacts of this truncation.
The measurement of relaxation rates to probe local molecular motions may be prohibitively long, especially for sensitivity-limited samples. In Chapter 5, a new method is introduced in which separating the dynamic and paramagnetic contributions to relaxation in paramagnetically doped samples can provide a picture of the molecular motions with significant time savings. This method is applied to a very large protein complex which is practically inaccessible to traditionally dynamical analyses.
The reduction in spin diffusion at fast MAS enables the measurement of site-specific relaxation on 13C’. In Chapter 6, it is found possible to gain insight into the local anisotropy of motions by comparing the dynamics as observed through 13C’ and 15N relaxation. Insight is gained into the types of motion affecting different secondary structure elements, and how the motions occurring may be related to intermolecular hydrogen-bonding interfaces, antibody recognition, and docking.
Item Type: | Thesis (PhD) | ||||
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Subjects: | Q Science > QC Physics Q Science > QD Chemistry |
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Library of Congress Subject Headings (LCSH): | Nuclear magnetic resonance, Solid state physics, Nuclear spin, Angular momentum (Nuclear physics) -- Coupling and recoupling, Molecular dynamics, Relaxation (Nuclear physics), Crystallography, Proteins | ||||
Official Date: | July 2023 | ||||
Dates: |
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Institution: | University of Warwick | ||||
Theses Department: | Department of Chemistry | ||||
Thesis Type: | PhD | ||||
Publication Status: | Unpublished | ||||
Supervisor(s)/Advisor: | Brown, Steven P. ; Lewandowski, Józef R. | ||||
Format of File: | |||||
Extent: | xxvii, 241 pages : illustrations | ||||
Language: | eng |
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