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  • About
  • The Global ETD Search service is a free service for researchers to find electronic theses and dissertations. This service is provided by the Networked Digital Library of Theses and Dissertations.
    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.
1

Structure determination of ribosomal proteins and development of new methods in biomolecular NMR

Helgstrand, Magnus January 2001 (has links)
This thesis concerns different areas of biomolecular nuclearmagnetic resonance spectroscopy (NMR). In the first part of thethesis a new formalism for simulations of NMR pulse sequencesis introduced. The formalism is derived both from classicalmechanics and quantum mechanics and is presented forhomonuclear and heteronuclear spin systems. The formalism hasalso been adapted to systems in chemical exchange. Simulationsof pulse sequences should be more straightforward using the newformalism. In the second part of the thesis the NMR solution structuresof two ribosomal proteins are described. The ribosome isresponsible for protein production in all living cells and tounderstand the mechanism of the ribosome it is important toknow the three dimensional structure. In this thesis thestructures of S16 and S19, two of the proteins in the smallribosomal subunit, are presented. S16 is a mixed α /βprotein with a five-stranded parallel-antiparallel β-sheetand two α -helices. S19 is s mixed α/β proteinwith a three-stranded parallel-antiparallel β -sheet, oneα -helix and a short 310-helix. In the third part of the thesis a program for semiautomaticassignment of NMR-spectra is presented. Assigning resonances inthe NMR spectrum is a labor-intensive process, which can takelong time. In semiautomatic assignment a computer program aidsthe user in finding assignments but leaves all decisions to theuser, thus speeding up the process. The program described inthis thesis is a new version of ANSIG, called Ansig forWindows. The program runs on PCs under Windows and has severaltools for semiautomatic assignment. <b>Keywords:</b>nuclear magnetic resonance, structuredetermination, ribosomal proteins, NMR simulations, NMR theory,NMR assignment software, semiautomatic assignment
2

Structure determination of ribosomal proteins and development of new methods in biomolecular NMR

Helgstrand, Magnus January 2001 (has links)
<p>This thesis concerns different areas of biomolecular nuclearmagnetic resonance spectroscopy (NMR). In the first part of thethesis a new formalism for simulations of NMR pulse sequencesis introduced. The formalism is derived both from classicalmechanics and quantum mechanics and is presented forhomonuclear and heteronuclear spin systems. The formalism hasalso been adapted to systems in chemical exchange. Simulationsof pulse sequences should be more straightforward using the newformalism.</p><p>In the second part of the thesis the NMR solution structuresof two ribosomal proteins are described. The ribosome isresponsible for protein production in all living cells and tounderstand the mechanism of the ribosome it is important toknow the three dimensional structure. In this thesis thestructures of S16 and S19, two of the proteins in the smallribosomal subunit, are presented. S16 is a mixed α /βprotein with a five-stranded parallel-antiparallel β-sheetand two α -helices. S19 is s mixed α/β proteinwith a three-stranded parallel-antiparallel β -sheet, oneα -helix and a short 3<sub>10</sub>-helix.</p><p>In the third part of the thesis a program for semiautomaticassignment of NMR-spectra is presented. Assigning resonances inthe NMR spectrum is a labor-intensive process, which can takelong time. In semiautomatic assignment a computer program aidsthe user in finding assignments but leaves all decisions to theuser, thus speeding up the process. The program described inthis thesis is a new version of ANSIG, called Ansig forWindows. The program runs on PCs under Windows and has severaltools for semiautomatic assignment.</p><p><b>Keywords:</b>nuclear magnetic resonance, structuredetermination, ribosomal proteins, NMR simulations, NMR theory,NMR assignment software, semiautomatic assignment</p>
3

Characterizing the pore structure of porous matrices using SEQ-NMR spectroscopy

Strömberg, Ella January 2020 (has links)
Characterization of the pore structure is a crucial part in themanufacturing of porous media used for purification of biologicalpharmaceuticals. This project took place at Cytiva in Uppsala and aimedat optimizing a newly developed method in pore structurecharacterization called size-exclusion quantification NMR (SEQ-NMR). Bymeasuring with diffusion NMR on a polymer solution before and afterequilibration with a material of interest the pore structure of thematerial can be determined. This project aimed at reducing the durationof a SEQ-NMR experiment while examining the performance of the methodduring different conditions with the goal of making the methodapplicable for quality control procedures. The method was optimizedboth by simulations and by experimental diffusion NMR measurements. Itwas discovered that the performance of the method could be improved byhaving an optimal mixture of the polymer solution and duringexperiments distributing ten measurement points with linear spacing.With these parameters optimized the duration of the method could bereduced with 22 hours landing on a total duration of 8 hours. Theduration combined with the complexity of the method still makes themethod unsuitable for use in quality control of porous media. Despitethe small possibility of SEQ-NMR being a quality control method thisproject has proven the method to be both reproducible and sensitive.

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