Current Crosslistings BIOC 5702
BIOC 5702
BIOC 3700
Analyze implications of molecular spectroscopy (absorption, emission, CD, NMR) results on polypeptide structure and environment in direct context of the physical basis of the technique in question. [BIOC 3700]
Analyze optical spectra (absorption, emission, fluorescence anisotropy, LD, CD, IR, Raman) with respect to polypeptide structure and environment and with relation to quantum mechanical basis of a given spectroscopic technique.Demonstrate understanding of hydrodynamic characterization by NMR (DOSY and spin relaxation), analytical ultracentrifugation and single molecule methods.Describe effects of spin-relaxation phenomena upon the experimental observable and the manner in which these are modulated by dynamic processes.Distinguish properties and behaviour of infrared vs. Raman active chromophores.Draw energy level diagrams showing the quantum mechanical basis of electronic absorption and emission spectroscopy with specific reference to the Franck-Condon principle.Use vector diagrams to explain the major NMR experiments employed for protein NMR.Compare and contrast ensemble measurements to single molecule measurements, with emphasis on experimental approaches allowing observation of single molecules and information uniquely obtainable by single molecule measurements.Assign two-dimensional homonuclear and heteronuclear NMR data for a polypeptide and apply these assignments for structure determination.Discriminate and quantify the components of the NMR Hamiltonian in terms of their contribution to the experimental observable in the solution- and solid-state.
