Learning objectives
The course has a practical formulation, to provide the students with advanced techniques and methodologies in the field of biophysics, in particular for the determination, prediction and analysis of the structure and the dynamics of proteic systems.
Prerequisites
Basic knowledge of the structure of biological macromolecules.
Course unit content
Search engines in biological databases. Protein and nucleic acid sequence analysis and sequence alignment tools. Secondary structure prediction and protein physico-chemical profiles.
Tertiary and quaternary structure of proteins and structure-activity relationship.
Experimental methods to determine the three-dimensional structure of proteins (NMR, X-ray diffractometry, atomic force microspopy). Spectroscopical techniques to study protein structure and function (fluorescence, circular dichroism, infrared spectroscopy).
Computational methods to predict the three-dimensional structure of proteins. Protein comparative modeling. Analysis of protein structure by means of molecular graphics softwares.
Molecular mechanics and force fields. Energy minimization. Molecular dynamics simulations. Molecular interaction: docking and drug design.
Full programme
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Bibliography
A.M. Lesk, "Introduzione alla Bioinformatica", McGraw-Hill Ed.
G. Valle, M. Helmer Citterich, M. Attimonelli, G. Pesole, "Introduzione alla Bioinformatica", Zanichelli Ed.
D.E. Krane, M.L. Raymer, "Fondamenti di Bioinformatica", Pearson Education Ed.
C.R. Cantor and P.R. Schimmel, "Biophysical chemistry - part II: techniques for the study of biological structure and function", W.H. Freeman and Company, San Francisco.
Notes on the lessons and review articles will be given by the lecturer.
Teaching methods
Oral lessons and practice in the laboratory.
Assessment methods and criteria
Discussions on the reports of the practical exercises. performed in the lab and oral examination.
Other information
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