Advanced search options

Advanced Search Options 🞨

Browse by author name (“Author name starts with…”).

Find ETDs with:

in
/  
in
/  
in
/  
in

Written in Published in Earliest date Latest date

Sorted by

Results per page:

Sorted by: relevance · author · university · dateNew search

You searched for +publisher:"University of Guelph" +contributor:("Ladizhansky, Vladimir"). Showing records 1 – 11 of 11 total matches.

Search Limiters

Last 2 Years | English Only

No search limiters apply to these results.

▼ Search Limiters


University of Guelph

1. Ritz, Emily. Site-Specific Solid-State NMR Studies of the Protein-Water Interface of Anabaena Sensory Rhodopsin.

Degree: MS, Department of Physics, 2012, University of Guelph

 Solid-state NMR spectroscopy was used to site-specifically investigate the protein-water interface of a seven alpha-helical transmembrane protein, Anabaena sensory rhodopsin (ASR). Water-edited experiments, which employ… (more)

Subjects/Keywords: solid-state NMR; rhodopsin; protein-water interactions; water-edited; biophysics; proton exchange; T2-filter

Record DetailsSimilar RecordsGoogle PlusoneFacebookTwitterCiteULikeMendeleyreddit

APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Ritz, E. (2012). Site-Specific Solid-State NMR Studies of the Protein-Water Interface of Anabaena Sensory Rhodopsin. (Masters Thesis). University of Guelph. Retrieved from https://atrium.lib.uoguelph.ca/xmlui/handle/10214/4006

Chicago Manual of Style (16th Edition):

Ritz, Emily. “Site-Specific Solid-State NMR Studies of the Protein-Water Interface of Anabaena Sensory Rhodopsin.” 2012. Masters Thesis, University of Guelph. Accessed October 29, 2020. https://atrium.lib.uoguelph.ca/xmlui/handle/10214/4006.

MLA Handbook (7th Edition):

Ritz, Emily. “Site-Specific Solid-State NMR Studies of the Protein-Water Interface of Anabaena Sensory Rhodopsin.” 2012. Web. 29 Oct 2020.

Vancouver:

Ritz E. Site-Specific Solid-State NMR Studies of the Protein-Water Interface of Anabaena Sensory Rhodopsin. [Internet] [Masters thesis]. University of Guelph; 2012. [cited 2020 Oct 29]. Available from: https://atrium.lib.uoguelph.ca/xmlui/handle/10214/4006.

Council of Science Editors:

Ritz E. Site-Specific Solid-State NMR Studies of the Protein-Water Interface of Anabaena Sensory Rhodopsin. [Masters Thesis]. University of Guelph; 2012. Available from: https://atrium.lib.uoguelph.ca/xmlui/handle/10214/4006


University of Guelph

2. Good, Daryl Byron. Conformational Dynamics in a Seven Transmembrane Protein Anabaena Sensory Rhodopsin Probed by Solid State NMR.

Degree: MS, Department of Physics, 2013, University of Guelph

 Solid state NMR spectroscopy can be used to probe internal motions in membrane proteins in a lipid environment. In this study the site-specific measurements of… (more)

Subjects/Keywords: membrane protein; rhodopsin; conformational dynamics; Anabaena Sensory Rhodopsin; solid state NMR

Record DetailsSimilar RecordsGoogle PlusoneFacebookTwitterCiteULikeMendeleyreddit

APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Good, D. B. (2013). Conformational Dynamics in a Seven Transmembrane Protein Anabaena Sensory Rhodopsin Probed by Solid State NMR. (Masters Thesis). University of Guelph. Retrieved from https://atrium.lib.uoguelph.ca/xmlui/handle/10214/7583

Chicago Manual of Style (16th Edition):

Good, Daryl Byron. “Conformational Dynamics in a Seven Transmembrane Protein Anabaena Sensory Rhodopsin Probed by Solid State NMR.” 2013. Masters Thesis, University of Guelph. Accessed October 29, 2020. https://atrium.lib.uoguelph.ca/xmlui/handle/10214/7583.

MLA Handbook (7th Edition):

Good, Daryl Byron. “Conformational Dynamics in a Seven Transmembrane Protein Anabaena Sensory Rhodopsin Probed by Solid State NMR.” 2013. Web. 29 Oct 2020.

Vancouver:

Good DB. Conformational Dynamics in a Seven Transmembrane Protein Anabaena Sensory Rhodopsin Probed by Solid State NMR. [Internet] [Masters thesis]. University of Guelph; 2013. [cited 2020 Oct 29]. Available from: https://atrium.lib.uoguelph.ca/xmlui/handle/10214/7583.

Council of Science Editors:

Good DB. Conformational Dynamics in a Seven Transmembrane Protein Anabaena Sensory Rhodopsin Probed by Solid State NMR. [Masters Thesis]. University of Guelph; 2013. Available from: https://atrium.lib.uoguelph.ca/xmlui/handle/10214/7583


University of Guelph

3. de Vlugt, Jeffrey. Identifying the Sugars and Phospholipids Tightly Bound to an Integral Membrane Protein.

Degree: MS, Department of Physics, 2019, University of Guelph

 Anabaena Sensory Rhodopsin (ASR) is a microbial photosensor found in cyanobacterium Anabaena sp. PCC 7120. It was found in previous studies that ASR co-purifies with… (more)

Subjects/Keywords: nuclear; magnetic; resonance; GlcNAc; Fuc4NAc; ManNAcA; solid-state NMR; solution NMR; 31P NMR; SSNMR; tightly-bound; co-purifies; ASR; anabaena; rhodopsin; constant-time; INEPT; TOBSY; DARR; CP; cross-polarization; insensitive nuclei enhanced by polarization transfer; phosphatidylethanolamine; PE; lipids; sugars; phospholipids; enterobacterial common antigen; ECA; integral; membrane; protein; E. coli; co-purification

Record DetailsSimilar RecordsGoogle PlusoneFacebookTwitterCiteULikeMendeleyreddit

APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

de Vlugt, J. (2019). Identifying the Sugars and Phospholipids Tightly Bound to an Integral Membrane Protein. (Masters Thesis). University of Guelph. Retrieved from https://atrium.lib.uoguelph.ca/xmlui/handle/10214/17386

Chicago Manual of Style (16th Edition):

de Vlugt, Jeffrey. “Identifying the Sugars and Phospholipids Tightly Bound to an Integral Membrane Protein.” 2019. Masters Thesis, University of Guelph. Accessed October 29, 2020. https://atrium.lib.uoguelph.ca/xmlui/handle/10214/17386.

MLA Handbook (7th Edition):

de Vlugt, Jeffrey. “Identifying the Sugars and Phospholipids Tightly Bound to an Integral Membrane Protein.” 2019. Web. 29 Oct 2020.

Vancouver:

de Vlugt J. Identifying the Sugars and Phospholipids Tightly Bound to an Integral Membrane Protein. [Internet] [Masters thesis]. University of Guelph; 2019. [cited 2020 Oct 29]. Available from: https://atrium.lib.uoguelph.ca/xmlui/handle/10214/17386.

Council of Science Editors:

de Vlugt J. Identifying the Sugars and Phospholipids Tightly Bound to an Integral Membrane Protein. [Masters Thesis]. University of Guelph; 2019. Available from: https://atrium.lib.uoguelph.ca/xmlui/handle/10214/17386


University of Guelph

4. Ward, Meaghan. Solid-State NMR Studies of Solvent-Accessible Fragments of a Seven-Helical Transmembrane Protein Proteorhodopsin.

Degree: MS, Department of Physics, 2011, University of Guelph

 High–resolution multidimensional proton-detected NMR was used to study the solvent-exposed regions of a seven-helical integral membrane proton pump proteorhodopsin (PR). Fully deuterated PR samples with… (more)

Subjects/Keywords: Proteorhodopsin; solid-state NMR; magic angle spinning; Double Quantum Coherence; membrane proteins; protein-water interaction

Record DetailsSimilar RecordsGoogle PlusoneFacebookTwitterCiteULikeMendeleyreddit

APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Ward, M. (2011). Solid-State NMR Studies of Solvent-Accessible Fragments of a Seven-Helical Transmembrane Protein Proteorhodopsin. (Masters Thesis). University of Guelph. Retrieved from https://atrium.lib.uoguelph.ca/xmlui/handle/10214/2970

Chicago Manual of Style (16th Edition):

Ward, Meaghan. “Solid-State NMR Studies of Solvent-Accessible Fragments of a Seven-Helical Transmembrane Protein Proteorhodopsin.” 2011. Masters Thesis, University of Guelph. Accessed October 29, 2020. https://atrium.lib.uoguelph.ca/xmlui/handle/10214/2970.

MLA Handbook (7th Edition):

Ward, Meaghan. “Solid-State NMR Studies of Solvent-Accessible Fragments of a Seven-Helical Transmembrane Protein Proteorhodopsin.” 2011. Web. 29 Oct 2020.

Vancouver:

Ward M. Solid-State NMR Studies of Solvent-Accessible Fragments of a Seven-Helical Transmembrane Protein Proteorhodopsin. [Internet] [Masters thesis]. University of Guelph; 2011. [cited 2020 Oct 29]. Available from: https://atrium.lib.uoguelph.ca/xmlui/handle/10214/2970.

Council of Science Editors:

Ward M. Solid-State NMR Studies of Solvent-Accessible Fragments of a Seven-Helical Transmembrane Protein Proteorhodopsin. [Masters Thesis]. University of Guelph; 2011. Available from: https://atrium.lib.uoguelph.ca/xmlui/handle/10214/2970


University of Guelph

5. Emami, Sanaz. Biophysical studies of human Aquaporin 1 Structural insights by Solid-State NMR and mechanism of inhibition by Mercury.

Degree: PhD, Department of Physics, 2016, University of Guelph

 Human Aquaporin 1 (hAQP1) is a membrane protein that transfers water across the membrane with a rate faster than that of the simple diffusion. This… (more)

Subjects/Keywords: Human Aquaporin 1; Solid-state NMR; Mercury; Inhibition

Record DetailsSimilar RecordsGoogle PlusoneFacebookTwitterCiteULikeMendeleyreddit

APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Emami, S. (2016). Biophysical studies of human Aquaporin 1 Structural insights by Solid-State NMR and mechanism of inhibition by Mercury. (Doctoral Dissertation). University of Guelph. Retrieved from https://atrium.lib.uoguelph.ca/xmlui/handle/10214/9484

Chicago Manual of Style (16th Edition):

Emami, Sanaz. “Biophysical studies of human Aquaporin 1 Structural insights by Solid-State NMR and mechanism of inhibition by Mercury.” 2016. Doctoral Dissertation, University of Guelph. Accessed October 29, 2020. https://atrium.lib.uoguelph.ca/xmlui/handle/10214/9484.

MLA Handbook (7th Edition):

Emami, Sanaz. “Biophysical studies of human Aquaporin 1 Structural insights by Solid-State NMR and mechanism of inhibition by Mercury.” 2016. Web. 29 Oct 2020.

Vancouver:

Emami S. Biophysical studies of human Aquaporin 1 Structural insights by Solid-State NMR and mechanism of inhibition by Mercury. [Internet] [Doctoral dissertation]. University of Guelph; 2016. [cited 2020 Oct 29]. Available from: https://atrium.lib.uoguelph.ca/xmlui/handle/10214/9484.

Council of Science Editors:

Emami S. Biophysical studies of human Aquaporin 1 Structural insights by Solid-State NMR and mechanism of inhibition by Mercury. [Doctoral Dissertation]. University of Guelph; 2016. Available from: https://atrium.lib.uoguelph.ca/xmlui/handle/10214/9484


University of Guelph

6. Ward, Meaghan Elizabeth. Solid-State NMR Investigations of Transmembrane Proteins - New Approaches for Signal Enhancement and In Situ Studies of Anabaena Sensory Rhodopsin.

Degree: PhD, Department of Physics, 2016, University of Guelph

 Membrane proteins account for 30% of all proteins and perform many important roles in the cell, yet are difficult to study due to the necessity… (more)

Subjects/Keywords: solid state nuclear magnetic resonance; membrane protein; proton detection; In situ; microbial rhodopsin; magic angle spinning; paramagnetic relaxation; condensed data collection

Record DetailsSimilar RecordsGoogle PlusoneFacebookTwitterCiteULikeMendeleyreddit

APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Ward, M. E. (2016). Solid-State NMR Investigations of Transmembrane Proteins - New Approaches for Signal Enhancement and In Situ Studies of Anabaena Sensory Rhodopsin. (Doctoral Dissertation). University of Guelph. Retrieved from https://atrium.lib.uoguelph.ca/xmlui/handle/10214/9784

Chicago Manual of Style (16th Edition):

Ward, Meaghan Elizabeth. “Solid-State NMR Investigations of Transmembrane Proteins - New Approaches for Signal Enhancement and In Situ Studies of Anabaena Sensory Rhodopsin.” 2016. Doctoral Dissertation, University of Guelph. Accessed October 29, 2020. https://atrium.lib.uoguelph.ca/xmlui/handle/10214/9784.

MLA Handbook (7th Edition):

Ward, Meaghan Elizabeth. “Solid-State NMR Investigations of Transmembrane Proteins - New Approaches for Signal Enhancement and In Situ Studies of Anabaena Sensory Rhodopsin.” 2016. Web. 29 Oct 2020.

Vancouver:

Ward ME. Solid-State NMR Investigations of Transmembrane Proteins - New Approaches for Signal Enhancement and In Situ Studies of Anabaena Sensory Rhodopsin. [Internet] [Doctoral dissertation]. University of Guelph; 2016. [cited 2020 Oct 29]. Available from: https://atrium.lib.uoguelph.ca/xmlui/handle/10214/9784.

Council of Science Editors:

Ward ME. Solid-State NMR Investigations of Transmembrane Proteins - New Approaches for Signal Enhancement and In Situ Studies of Anabaena Sensory Rhodopsin. [Doctoral Dissertation]. University of Guelph; 2016. Available from: https://atrium.lib.uoguelph.ca/xmlui/handle/10214/9784


University of Guelph

7. Bolton, David. Amide proton assignments of partially deuterated Anabaena Sensory Rhodopsin, investigation of solvent exchangeability and deuterium isotope effects.

Degree: MS, Department of Physics, 2017, University of Guelph

 Magic angle spinning solid-state NMR has been used with great success in studying membrane proteins in a native-like environment. These typically carbon-detected experiments are very… (more)

Record DetailsSimilar RecordsGoogle PlusoneFacebookTwitterCiteULikeMendeleyreddit

APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Bolton, D. (2017). Amide proton assignments of partially deuterated Anabaena Sensory Rhodopsin, investigation of solvent exchangeability and deuterium isotope effects. (Masters Thesis). University of Guelph. Retrieved from https://atrium.lib.uoguelph.ca/xmlui/handle/10214/11589

Chicago Manual of Style (16th Edition):

Bolton, David. “Amide proton assignments of partially deuterated Anabaena Sensory Rhodopsin, investigation of solvent exchangeability and deuterium isotope effects.” 2017. Masters Thesis, University of Guelph. Accessed October 29, 2020. https://atrium.lib.uoguelph.ca/xmlui/handle/10214/11589.

MLA Handbook (7th Edition):

Bolton, David. “Amide proton assignments of partially deuterated Anabaena Sensory Rhodopsin, investigation of solvent exchangeability and deuterium isotope effects.” 2017. Web. 29 Oct 2020.

Vancouver:

Bolton D. Amide proton assignments of partially deuterated Anabaena Sensory Rhodopsin, investigation of solvent exchangeability and deuterium isotope effects. [Internet] [Masters thesis]. University of Guelph; 2017. [cited 2020 Oct 29]. Available from: https://atrium.lib.uoguelph.ca/xmlui/handle/10214/11589.

Council of Science Editors:

Bolton D. Amide proton assignments of partially deuterated Anabaena Sensory Rhodopsin, investigation of solvent exchangeability and deuterium isotope effects. [Masters Thesis]. University of Guelph; 2017. Available from: https://atrium.lib.uoguelph.ca/xmlui/handle/10214/11589

8. Brown, Rachel Ellen. Adaptation of Green Proteorhodopsin to Changes in Membrane Lipid Composition.

Degree: MS, Department of Physics, 2018, University of Guelph

 The protein studied in this thesis is Proteorhodopsin (PR), which is linked to starvation states in marine bacteria. This work examines PR membrane system stability… (more)

Subjects/Keywords: Proteorhodopsin; Membrane Properties; NMR; FTIR

Record DetailsSimilar RecordsGoogle PlusoneFacebookTwitterCiteULikeMendeleyreddit

APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Brown, R. E. (2018). Adaptation of Green Proteorhodopsin to Changes in Membrane Lipid Composition. (Masters Thesis). University of Guelph. Retrieved from https://atrium.lib.uoguelph.ca/xmlui/handle/10214/14219

Chicago Manual of Style (16th Edition):

Brown, Rachel Ellen. “Adaptation of Green Proteorhodopsin to Changes in Membrane Lipid Composition.” 2018. Masters Thesis, University of Guelph. Accessed October 29, 2020. https://atrium.lib.uoguelph.ca/xmlui/handle/10214/14219.

MLA Handbook (7th Edition):

Brown, Rachel Ellen. “Adaptation of Green Proteorhodopsin to Changes in Membrane Lipid Composition.” 2018. Web. 29 Oct 2020.

Vancouver:

Brown RE. Adaptation of Green Proteorhodopsin to Changes in Membrane Lipid Composition. [Internet] [Masters thesis]. University of Guelph; 2018. [cited 2020 Oct 29]. Available from: https://atrium.lib.uoguelph.ca/xmlui/handle/10214/14219.

Council of Science Editors:

Brown RE. Adaptation of Green Proteorhodopsin to Changes in Membrane Lipid Composition. [Masters Thesis]. University of Guelph; 2018. Available from: https://atrium.lib.uoguelph.ca/xmlui/handle/10214/14219


University of Guelph

9. Dingwell, Dylan Archer. Refinement of Loop Structure in Human Aquaporin-1 by Solid-State NMR Spectroscopy.

Degree: MS, Department of Physics, 2019, University of Guelph

 Human aquaporin-1 (hAQP1) is a channel protein which selectively facilitates translocation of water across the cell membrane, serving important physiological functions including epithelial fluid transport… (more)

Subjects/Keywords: solid-state nmr; nmr; aquaporin; membrane proteins

Record DetailsSimilar RecordsGoogle PlusoneFacebookTwitterCiteULikeMendeleyreddit

APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Dingwell, D. A. (2019). Refinement of Loop Structure in Human Aquaporin-1 by Solid-State NMR Spectroscopy. (Masters Thesis). University of Guelph. Retrieved from https://atrium.lib.uoguelph.ca/xmlui/handle/10214/16214

Chicago Manual of Style (16th Edition):

Dingwell, Dylan Archer. “Refinement of Loop Structure in Human Aquaporin-1 by Solid-State NMR Spectroscopy.” 2019. Masters Thesis, University of Guelph. Accessed October 29, 2020. https://atrium.lib.uoguelph.ca/xmlui/handle/10214/16214.

MLA Handbook (7th Edition):

Dingwell, Dylan Archer. “Refinement of Loop Structure in Human Aquaporin-1 by Solid-State NMR Spectroscopy.” 2019. Web. 29 Oct 2020.

Vancouver:

Dingwell DA. Refinement of Loop Structure in Human Aquaporin-1 by Solid-State NMR Spectroscopy. [Internet] [Masters thesis]. University of Guelph; 2019. [cited 2020 Oct 29]. Available from: https://atrium.lib.uoguelph.ca/xmlui/handle/10214/16214.

Council of Science Editors:

Dingwell DA. Refinement of Loop Structure in Human Aquaporin-1 by Solid-State NMR Spectroscopy. [Masters Thesis]. University of Guelph; 2019. Available from: https://atrium.lib.uoguelph.ca/xmlui/handle/10214/16214

10. Park, Hansul David. Development of a perdeuteration protocol to study yeast-produced eukaryotic membrane proteins using solid-state NMR spectroscopy.

Degree: MS, Department of Physics, 2017, University of Guelph

 A number of obstacles exist in the study of eukaryotic membrane protein structure using solid- state NMR. Firstly, although bacterial hosts are often used to… (more)

Subjects/Keywords: yeast; solid-state nmr; deuteration; nmr

Record DetailsSimilar RecordsGoogle PlusoneFacebookTwitterCiteULikeMendeleyreddit

APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Park, H. D. (2017). Development of a perdeuteration protocol to study yeast-produced eukaryotic membrane proteins using solid-state NMR spectroscopy. (Masters Thesis). University of Guelph. Retrieved from https://atrium.lib.uoguelph.ca/xmlui/handle/10214/11380

Chicago Manual of Style (16th Edition):

Park, Hansul David. “Development of a perdeuteration protocol to study yeast-produced eukaryotic membrane proteins using solid-state NMR spectroscopy.” 2017. Masters Thesis, University of Guelph. Accessed October 29, 2020. https://atrium.lib.uoguelph.ca/xmlui/handle/10214/11380.

MLA Handbook (7th Edition):

Park, Hansul David. “Development of a perdeuteration protocol to study yeast-produced eukaryotic membrane proteins using solid-state NMR spectroscopy.” 2017. Web. 29 Oct 2020.

Vancouver:

Park HD. Development of a perdeuteration protocol to study yeast-produced eukaryotic membrane proteins using solid-state NMR spectroscopy. [Internet] [Masters thesis]. University of Guelph; 2017. [cited 2020 Oct 29]. Available from: https://atrium.lib.uoguelph.ca/xmlui/handle/10214/11380.

Council of Science Editors:

Park HD. Development of a perdeuteration protocol to study yeast-produced eukaryotic membrane proteins using solid-state NMR spectroscopy. [Masters Thesis]. University of Guelph; 2017. Available from: https://atrium.lib.uoguelph.ca/xmlui/handle/10214/11380

11. O'Halloran, Matthew. Use of a Paramagnetic Spin Label for Determination of Long-Range Distance Constraints in Solid-State NMR.

Degree: MS, Department of Physics, 2014, University of Guelph

 Solid-State Nuclear Magnetic Resonance (SSNMR), with paramagnetic relaxation enhancement (PRE), is used to investigate the protein Proteorhodopsin (PR). PRE allows for the acquisition of long-range… (more)

Subjects/Keywords: Solid State Nuclear Magnetic Resonance (SSNMR); Paramagnetic Relaxation Enhancement (PRE); Membrane Proteins; Proteorhodopsin (PR); Site Specific Labelling

Record DetailsSimilar RecordsGoogle PlusoneFacebookTwitterCiteULikeMendeleyreddit

APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

O'Halloran, M. (2014). Use of a Paramagnetic Spin Label for Determination of Long-Range Distance Constraints in Solid-State NMR. (Masters Thesis). University of Guelph. Retrieved from https://atrium.lib.uoguelph.ca/xmlui/handle/10214/8278

Chicago Manual of Style (16th Edition):

O'Halloran, Matthew. “Use of a Paramagnetic Spin Label for Determination of Long-Range Distance Constraints in Solid-State NMR.” 2014. Masters Thesis, University of Guelph. Accessed October 29, 2020. https://atrium.lib.uoguelph.ca/xmlui/handle/10214/8278.

MLA Handbook (7th Edition):

O'Halloran, Matthew. “Use of a Paramagnetic Spin Label for Determination of Long-Range Distance Constraints in Solid-State NMR.” 2014. Web. 29 Oct 2020.

Vancouver:

O'Halloran M. Use of a Paramagnetic Spin Label for Determination of Long-Range Distance Constraints in Solid-State NMR. [Internet] [Masters thesis]. University of Guelph; 2014. [cited 2020 Oct 29]. Available from: https://atrium.lib.uoguelph.ca/xmlui/handle/10214/8278.

Council of Science Editors:

O'Halloran M. Use of a Paramagnetic Spin Label for Determination of Long-Range Distance Constraints in Solid-State NMR. [Masters Thesis]. University of Guelph; 2014. Available from: https://atrium.lib.uoguelph.ca/xmlui/handle/10214/8278

.