LEARNING OUTCOMES

The course teaches some techniques for the study of the physical properties of biological systems.

AIMS AND LEARNING OUTCOMES

The student will learn how to deal with complex biophysical problems, such as the self-assembly of biomolecules, the folding and unfolding of proteins and the transport processes through the cell membrane. The investigation will carried out at the molecular or single cell level.

At the end of the course the student will be able to:

- understand which experimental methods are best suited to study a particular biophysical process

- apply the acquired knowledge to design a biophysical experiment

- acquire the skills to conduct an experiment in the laboratory

- critically analyze the results of an experiment

The Biophysics Laboratory teaching can be chosen by students enrolled in the Master's Degree Course in Materials Science and Technology with particular reference to the "Materials Scientist: Research Specialist" profile.

PREREQUISITES

The course can be followed with profit by students who have obtained a three-year degree in a scientific field.

TEACHING METHODS

The course includes both lectures and laboratory experiences. Lectures are preparatory to the performance of laboratory experiences. For each laboratory experience, students are required to write a scientific report. Each report must contain an introductory part describing the state of the art, a part with the results obtained and a critical discussion of the results.

SYLLABUS/CONTENT

Scanning Tunneling Microscopy (STM): operating principle, scanning system, operation mode (constant current/height), resolution

Atomic Force Microscopy (AFM): operating principle, scanning system, operation mode (contact/tapping), resolution, force spectroscopy, nanolithography (nanoshaving and nanografting)

Optical microscopy: fluorescence, confocal and two-photon microscopy, operating principles, fluorescent probes, photobleaching, super-resolution techniques

Patch clamp technique for electrophysiological measurements: seal test, main configurations (whole cell, inside-out, outside-out, perforated patch), analysis of ionic currents

Protein crystallography: protein crystallization methods, outline of the methods used to determine the 3D structure of proteins

Laboratory experiences focus on the topics covered in the lectures. In particular:

- atomic force microscopy for the study of protein structures and thin organic films

- single-cell fluorescence microscopy for the study of intracellular calcium

- confocal and super-resolution microscopy

- patch clamp technique for the study of ionic currents across the cell membrane

- protein crystallization and crystal observation / manipulation

RECOMMENDED READING/BIBLIOGRAPHY

All the necessary material will be provided on Aulaweb