Novel postprocessing methods to remove the water resonance from protein NMR spectra [Elektronische Ressource] / vorgelegt von Kurt Stadlthanner

Novel Postprocessing Methodsto Remove the WaterResonance from Protein NMRSpectraDISSERTATION ZUR ERLANGUNG DESDOKTORGRADES DER NATURWISSENSCHAFTEN(DR. RER. NAT.) DER NATURWISSENSCHAFTLICHEN¨ ¨FAKULTAT II - PHYSIK DER UNIVERSITATREGENSBURGvorgelegt vonKurt Stadlthanneraus Regensburg2007Promotionsgesuch eingereicht am: 4. Juli 2007Die Arbeit wurde angeleitet von: Prof. Dr. Elmar LangPru¨fungsausschuss:Vorsitzender: Prof. Dr. J. Zweck1. Gutachter: Prof. Dr. E. W. Lang2. Gutachter: Prof. Dr. A. M. Tom´e3. Gutachter: Prof. Dr. I. Morgensternto NatachaivSummaryNMR spectroscopy is one of the most popular tools used in the spatial struc-ture determination of proteins. It owes much of its popularity to the factthat it is the only method with which proteins can be investigated under1quasi-physiological conditions. However, if the behavior of the H-protonsof the proteins is studied in an NMR experiment a dominant water signalis observed which exacerbates the automated analysis of the recorded dataconsiderably.The water resonance appears as the proteins under investigation are usu-ally dissolved in water in order to analyze them under quasi-physiologicalconditions. In such experiments the concentration of the proteins in water1is usually very low such that the recorded H-NMR spectra contain mostlythe resonance signal of the water protons while the resonances of the pro-tein protons can hardly be resolved.