General Physics, Biochemistry of Proteins, Nucleic Acids and Lipids.
In the theoretical classes (T) the main subjects from the UC´s program will be taught, using suitable audio-visual methodologies and internet access. Active participation from the students will be strongly encouraged.
In the theoretical-practical sessions (TP) the students will be trained in problem solving to solve and spectra interpretation ("dry labs") associated with the techniques taught at the theoretical classes, previously presented to the students via the internet ("infodocente"), in order to develop the capacity of the student for solving practical problems.
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, Biophysics, 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 and phosphorescence, quantum yields, quenching.
Resolution Problems: 10.0%
Mini Tests: 20.0%
I.A. Kaltashov and S.J. Eyles (2005) Mass Spectrometry in Biophysics: Conformation and Dynamics of Biomolecules Willey and Sons, Inc.
F. Siebert and P. Hildebrandt (2007) Vibrational spectroscopy in Life Sciences, Wiley.
J.M. Hollas (2004) Modern Spectroscopy, 4th ed.,Wiley.
V.M.S. Gil and C.F.G.C. Geraldes (2002) Ressonância Magnética Nuclear- Fundamentos, Métodos e Aplicações, Fundação Calouste Gulbenkian, 2nd ed., Lisboa.
I.D. Campbell and R.A. Dwek(1984) Biological Spectroscopy, Benjamin, Menlo Park, California..
K.E. Van Holde (1985) Physical Biochemistry, Prentice Hall, N. Jersey.
C. R. Cantor and P.R. Schimmel (1980) Biophysical Chemistry, Part II: Techniques for the Study of Biological Structure and Function, Freeman, New York.
R.S. Drago(1992) Physical Methods for Chemists, Saunders, Ft. Worth.
K. Wüthrich (1986) NMR of Proteins and Nucleic Acids, Willey and Sons, Inc.
J. Keeler (2005) Understanding NMR Spectroscopy, Willey and Sons, Inc.
J.N.S Evans (1995) Biomolecular NMR Spectroscopy, Oxford University Press.