About This Course

NMR: physical background for NMR: nuclear spin, spin in a magnetic field, CW-NMR, FT-NMR, radiofrequency pulses; Spectral Parameters: chemical shift, scalar and dipolar coupling,; spectroscopic techniques: 1D eksperiments with one or more pulses; practical aspects: construction of NMR spectrometers, practical eksperimental NMR, signal handling, nuclear magnetic relaxation: spin-lattice og spin-spin relaxation and their dependence on molecular mobility, nuclear Overhauser effect.; 2D-NMR: 'chemical shift labelling', magnetization transfer between spins, creation of the second dimension, homonuclear 2D (COSY, TOCSY, NOESY), heteronuclear 2D (HSQC, HMQC); Dynamic NMR Spectroscopy: chemical exchange, lineshape analysis, coalescence, time-scale of NMR, use of pulsed-field gradients in NMR, Diffusion-Ordered Spectroscopy, Interpretation of NMR Spectra: assignment of signals, structure determination of small molecules, metabolic profiling by NMR; Exercises: spectrum interpretation, identification of unknown compounds from NMR spectrometer, hands-on recording of NMR spectra, theretical calculations.

MS: History of MS development and application possibilites within Life Scienes, Biotechnology and chemistry. Physcial principles behind MS ionization (matrix-assisted laser desorption ionoization/elektro-spray); mass analyzers (time-of flight, quadrupol, ion-trap, Orbitrap).  MS/MS sequencing, ion detection, reflectron. Application of on-line chrmomatography (HPLC, GC, CE). Specific applications of MS: MALDI-TOF-MS og nano-spray followed by MS/MS for protein analyses. Interpretation of MS spectra of organic molecules, proteins, peptides and DNA, carbohydrates. and theoretical calculations. Application of MS for targeted og untargeted metabolomics og proteomics. Introduction to MS-based bioinformatics..