This CU has the objective of training the students in the basic concepts of the most important spectroscopic techniques, the capacity of interpreting basic spectra of simple molecules and the way the spectroscopic parameters are used in structural biochemistry. Some of these techniques are also fundamental in medical imaging applications. The spectroscopic techniques covered are: nuclear magnetic resonance (NMR) and electron paramagnetic resonance (EPR), electronic absorption spectroscopy, circular dicrosim, luminescence, vibrational spectroscopy (IR absorption, Raman and INS), X-ray diffraction and mass spectrometry. Thus, the student will be able to apply the basic spectroscopic techniques to the identification, as well asstructural and dynamical characterizaton of biomolecules.
Introduction to molecular spectroscopy. Interaction of radiation with matter. Types of spectroscopies: NMR, EPR, Electronic absorption (UV-Vis), circular dicroism, luminescence, vibrational ? IR and Raman (normal and resonance), Light scattering - Rayleigh inelastic, dynamic and Raman (normal and resonance), electron diffraction, electron microscopy and mass spectrometry. For each technique: physical basis, spectral parameters and interpretation, applications in Biochemistry, Byophysics, Biology and Medicine. As examples, the following are shown in more detail. NMR: examples in biological systems: proteins, nucleic acids and biomembranes. Metabolic and clinical studies. Introduction to MRI. Contrast agents. In EPR: Spin traps, spin probes, metalloproteins. In Uv-VIS: chromophores, selection rules and band intensities, hypochromism, optical activity of ORD and CD bands. In luminescence: fluorescence an phosphorescence, quantum yields, quenching.
Physics, Introductory Biochemistry, Biochemsitry I
Generic skills to reach
(by decreasing order of importance)
Teaching hours per semester
total of teaching hours
Bibliography of reference
- ?Ressonância Magnética Nuclear- Fundamentos, Métodos e Aplicações?, V.M.S. Gil e C.F.G.C. Geraldes, Fundação Calouste Gulbenkian, 2.ª edição, Lisboa, 2002
- ?Physical Biochemistry?, K.E. Van Holde, Prentice Hall, N. Jersey, 1985.
- ?Biophysical Chemistry, Part II: Techniques for the Study of Biological Structure and Function?, C: R. Cantor e P. R. Schimmel, Freeman, New York, 1980.
- ?Physical Methods for Chemists?, R.S. Drago, Saunders, Ft. Worth, 1992.
- ?Biomolecular NMR Spectroscopy?, J.N.S Evans, Oxford University Press (1995)
- ?Fundamentals of Protein NMR Spectroscopy in Structural Biology?, G.S. Rule e T.K. Hitchens, Springer (2005)
- ?Protein NMR for the Millenium?, N.R. Krishna, L.J. Berliner, Springer (2003).
?Mass Spectrometry in Biophysics: Conformation and Dynamics of Biomolecules?, Kaltashov I. A. e Eyles S. J., Willey and Sons, Inc., 2005.
- Vibrational spectroscopy in Life Sciences - Friedrich Siebert and Peter Hildebrandt, Wiley 2007
- theoretical (T): the main subjects from the UC´s program will be taught, using suitable audio-visual methodologies and internet. Active participation from the students will be strongly encouraged.
- theoretical-practical (TP): students solve problems and interpret spectra (dry lab) associated with the techniques taught at the theoretical classes. The classes have a tutorial nature, with the participation in the teaching and clarification of doubts of the students of the Master course in Biochemistry.
- the capacity of the student for solving practical problems the fundamental objective