INTRODUCTION TO BIOPHYSICS
cod. 1001234

Academic year 2009/10
1° year of course - Second semester
Professor
Academic discipline
Fisica applicata (a beni culturali, ambientali, biologia e medicina) (FIS/07)
Field
Sperimentale applicativo
Type of training activity
Characterising
72 hours
of face-to-face activities
9 credits
hub:
course unit
in - - -

Learning objectives

Biophysics is an interdisciplinary science that employs and develops theories and methods of the physical sciences for the investigation of biological systems at all level of organization: from the molecular scale, to entire organisms, up to ecosystems. Biophysical research shares thus significant overlap with the more specific fields of biochemistry, nanotechnology, bioengineering, and the more recent area of system biology. Aim of the corse is to furnish an overview of biophysical topics, with a deep insight into selected topics.

Prerequisites

- - -

Course unit content

 Programme<br />
A. The basics I: level of structure in biosystems. Elementary constituents, macromolecules, cellular structures and organelles, supercellular structures (e.g. biofilm, colonies, tissues), organisms and life domains, ecosystems. Structural levels of proteins, nucelic acids, cellular and intracellular membranes.<br />
B. The basics II: physical chemistry unit. Thermodynamics and thermodynamic functions. Spontaneity of reaction. Chemical equlibria. Reaction kinetics. Redox reactions, proton and electron transfer reactions. Photo-induced reactions and their thermodynamic aspects.<br />
C. Structure and function of biological macromolecules. Protein synthesis. Folding of proteins, kinetic and thermodynamic aspects. Post-translational modifications. Association, dissociation, assembly. Conformations and sub-conformations. Protein reactions: mechanism, kinetics and thermodynamics. Co-factors and prothestic groups.Binding theory and cooperativity. Structural transitions, regolation and allostery. Enzymes and molecular machines. Enzyme kinetics. Nucleic acids. <br />
D. Techniques for the investigation of protein tridimensional structure. NMR, X-ray and other diffraction techniques. Spectroscopies for the study of preotein structure and function. Protein modeling. .<br />
E. Photobiology unit. Light as energy and information. Structure and reactivity of chromophores. Maolecular energy transfer. Primitive photosynthesis by light-driven ion pumps. Oxygenic and anoxygenic photosynthesis. Photosensory receptor systems: visual processes, photosensory receptors in plant and bacteria. Biological effects of electromagentic radiation and photosensitization. <br />
F. Input-output: sensor proteins and biological responses. Intrinsic and extrinsic membrane proteins, two-component systems, modular organization of sensory proteins. Molecular mechanisms of signal transduction: protein conformational changes, molecular transducers and second messengers. Examples from chemo- and photo-induced signaling chains. Examples from the three life-domains: Eukarya, Bacteria, Archaea. <br />
G. New-trends: Engineering of proteins as reporters for cellular studies and as regulators for metabolite´s concentration. Single molecule spectroscopy. Introduction to environmental biophysics. Introduction to system biology.

Full programme

- - -

Bibliography

Lesson material plus articles assigned during the course.

Teaching methods

Frontal  lessons with slides. Written exams with questions.

Assessment methods and criteria

- - -

Other information

- - -