Learning objectives
<span lang=""EN-US"" new="" font-family:="" style="">To provide physics students interested to study biological systems the basic biochemical and biophysical experimental techniques.</span>
Prerequisites
<span lang=""EN-US"" new="" font-family:="" style="">Basic Physics<br />
Inorganic and organic chemistry<br />
Principles of quantum mechanics<br />
</span>
Course unit content
<p><span lang=""EN-US"" new="" font-family:="" style="">Water: the molecule, hydrogen bond, water phases. Aqueous solutions: ionic solutions, acids, bases, pH, measurement of pH. Solutions of macromolecules: proteins, partial molar and partial specific quantities, chemical potential, nonideal behaviour in solution of macromolecules, the second virial coefficient, sources of nonideality. Purification of a proteic solution: filtration, dialysis, centrifugation, lyophilization. Analysis of a solution of proteins: spectroscopic analysis.<br />
Energy levels of a molecule. Electromagnetic spectrum. Interaction of light and matter. UV-Vis spectroscopy: electronic levels. Einstein coefficient for absorption. Lambert-Beer law. Extinction coefficient. Double beam spectrophotometer. Single beam spectrophotometer for fast kinetics. Characters of the absorption spectra. Spectroscopy applied to biological macromolecules: formaldehyde, peptidic bond, chromophores, prosthetic groups, solvent effects. IR spectroscopy: transition dipole moment, vibrational transitions. FTIR specrophotometer: principles and advantages. Samples for IR spectroscopy. Analysis of the IR spectra. IR absorption spectra of proteins: amide bands. The problem of water. ATR technique.</span></p>
<p><span lang=""EN-US"" new="" font-family:="" style=""><u>Laboratory experiences</u><br />
Titration of a strong, a weak and a threeprotic acid.<br />
Titration of an aminoacid and of a protein.<br />
Preparation of buffer solutions.<br />
Extraction of casein and lactoglobulin from milk.<br />
Check of Lambert-Beer law. <br />
Biureto test.<br />
Spectrophotometric titration.<br />
Activity test of an enzyme.<br />
IR analysis of water content in a protein .<br />
IR analysis of the secondary structure of a protein in the native and denatured state</span></p>
Bibliography
<span lang="""EN-US""" style="" font-family:="""" new="""">C.R. Cantor and P.R. Schimmel BIOPHYSICAL CHEMISTRY- part II - </span><span lang="""EN-US""" style="" font-family:="""" new="""">W.H. Freeman and Co, Eds. San Francisco<br />
</span><span lang="""EN-US""" style="" font-family:="""" new="""">K. E. Van Holde PHYSICAL BIOCHEMISTRY Prentice-Hall, Inc., New Jersey</span><br />
<span lang="""EN-US""" style="" font-family:="""" new=""""></span>
Teaching methods
<span lang=""EN-US"" new="" font-family:="" style="">Teaching metodology: frontal lectures and exercises. Practical laboratory.<br />
</span><span lang=""EN-US"" new="" font-family:="" style="">Examination metodology: oral examination with discussion of the laboratory experiences.</span>
