ID:
501316
Duration (hours):
64
CFU:
6
SSD:
BIOCHIMICA
Year:
2025
Overview
Date/time interval
Secondo Semestre (02/03/2026 - 19/06/2026)
Syllabus
Course Objectives
The course aims to describe theoretical basis and practical application of the main experimental techniques used in biochemistry and biomolecular research. At the end of the course students will have detailed information necessary to address the common theoretical and practical issues occurring during planning and execution of experiments.
Course Prerequisites
The understanding of the topics covered in the Applied Biochemistry course requires the student to have knowledge of Organic Chemistry, in particular concerning the main functional groups and the structure of heterocyclic compounds, as well as knowledge of spectroscopic techniques applied to the study of organic molecules. It is also essential to have knowledge of Biochemistry regarding the structure and properties of amino acids, proteins and nucleic acids; these skills can be acquired by following the General Biochemistry course held in the second semester in parallel with the Applied Biochemistry course. It is only possible to take the Applied Biochemistry examination after passing the Organic Chemistry I examination.
Teaching Methods
The course involves face to face lectures (32 hours) and laboratory practice (32 hours). Classroom lectures are provided with the support of power point slides and video. PDF of slides and other material presented during the lectures will be uploaded on the KIRO platform. During the laboratory practice, students will be divided into small groups and will perform their own experiments following detailed protocols. Further support for students will be provided by tutors who will be present in the laboratory. Attendance at practical activities is mandatory.
The teacher is available for further explanations on specific topics upon request.
For students with special needs, who cannot attend teaching activities in person and who have applied for Inclusive Teaching Modalities, suitable teaching materials will be available for fruitful self-study. If required, tutoring or supplementary teaching activities, remote or face to face meetings may be provided to support their self-learning.
The teacher is available for further explanations on specific topics upon request.
For students with special needs, who cannot attend teaching activities in person and who have applied for Inclusive Teaching Modalities, suitable teaching materials will be available for fruitful self-study. If required, tutoring or supplementary teaching activities, remote or face to face meetings may be provided to support their self-learning.
Assessment Methods
The course involves oral examination in any of the established examination dates. The exam will be based on at least three different topics covered during the course (both lectures and practice). During the assessment students must show that they have learnt and understood the topics of the course, that they have achieved good communication skills with appropriate scientific terminology.
Appropriate examination modalities are foreseen for students who fall into the categories of Specific Learning Disorders (SLDs) and Special Educational Needs (SEN)'.
Appropriate examination modalities are foreseen for students who fall into the categories of Specific Learning Disorders (SLDs) and Special Educational Needs (SEN)'.
Texts
Stoppini M. e Bellotti V. “Biochimica Applicata”. EdiSES
MC Bonaccorsi Di Patti, R Contestabile, ML Di Salvo. ”Metodologie biochimiche”. Zanichelli
M Maccarrone. “Metodologie biochimiche e biomolecolari”. Zanichelli
Wilson & Wolker. “Biochimica e Biologia molecolare principi e tecniche”. Raffaello Cortina Editore
MC Bonaccorsi Di Patti, R Contestabile, ML Di Salvo. ”Metodologie biochimiche”. Zanichelli
M Maccarrone. “Metodologie biochimiche e biomolecolari”. Zanichelli
Wilson & Wolker. “Biochimica e Biologia molecolare principi e tecniche”. Raffaello Cortina Editore
Contents
Theoretical part of the course
Theoretical principles and instrument description are presented for each experimental technique; then examples of practical application are described.
Methods of tissue homogenization for protein extraction.
Basic principles of centrifugation. Coefficient of sedimentation. Instrumentation for centrifugation.
Methods of precipitation in the early steps of protein purification. Dialysis and ultrafiltration.
Chromatography: general principles. Column-based types of chromatography for separation of biomolecules. Ion-exchange chromatography, gel filtration, affinity chromatography, hydrophobic interaction chromatography, partition chromatography. HPLC. FPLC.
Electrophoresis: general principles. Methods of protein electrophoresis: polyacrylamide gel electrophoresis (PAGE), SDS-PAGE, isoelectrofocusing, two-dimensional electrophoresis, capillary electrophoresis. Analysis of serum proteins by native electrophoresis.
Spectroscopic analysis of proteins. Ultraviolet-visible absorption spectroscopy. Spectrofluorimetry. Circular dichroism spectroscopy. Applications of spectroscopic techniques for studying protein structure, thermodynamic stability and folding.
Mass spectrometry. Ionization and analysis of proteins by mass spectrometry. Basic concepts of proteomics.
Production of polyclonal and monoclonal antibodies. Immunochemical techniques: ELISA, western blotting, immunodiffusion.
Study of protein-ligand interaction. Biacore.
Extraction and purification of nucleic acids. Quantification of nucleic acids. Electrophoresis of nucleic acids.
Restriction enzymes and cloning techniques.
DNA amplification by polymerase chain reaction (PCR). Reverse transcription polymerase chain reaction (RT-PCR) and quantitative PCR. Production of complementary DNA (cDNA).
DNA sequencing.
Plasmid vectors for gene cloning and expression.
Strategies for the expression of recombinant proteins. Production of recombinant proteins as native proteins, inclusion bodies and fusion proteins. Site directed mutagenesis.
Laboratory practice topics
Salting out of proteins using ammonium sulfate precipitation.
Dialysis.
Measurement of protein solutions by Biuret assay.
Ion-exchange chromatography.
Serum proteins electrophoresis.
SDS-PAGE.
Western blotting.
Enzymatic measurement of glucose.
DNA extraction from blood.
PCR
Agarose gel electrophoresis of DNA.
Theoretical principles and instrument description are presented for each experimental technique; then examples of practical application are described.
Methods of tissue homogenization for protein extraction.
Basic principles of centrifugation. Coefficient of sedimentation. Instrumentation for centrifugation.
Methods of precipitation in the early steps of protein purification. Dialysis and ultrafiltration.
Chromatography: general principles. Column-based types of chromatography for separation of biomolecules. Ion-exchange chromatography, gel filtration, affinity chromatography, hydrophobic interaction chromatography, partition chromatography. HPLC. FPLC.
Electrophoresis: general principles. Methods of protein electrophoresis: polyacrylamide gel electrophoresis (PAGE), SDS-PAGE, isoelectrofocusing, two-dimensional electrophoresis, capillary electrophoresis. Analysis of serum proteins by native electrophoresis.
Spectroscopic analysis of proteins. Ultraviolet-visible absorption spectroscopy. Spectrofluorimetry. Circular dichroism spectroscopy. Applications of spectroscopic techniques for studying protein structure, thermodynamic stability and folding.
Mass spectrometry. Ionization and analysis of proteins by mass spectrometry. Basic concepts of proteomics.
Production of polyclonal and monoclonal antibodies. Immunochemical techniques: ELISA, western blotting, immunodiffusion.
Study of protein-ligand interaction. Biacore.
Extraction and purification of nucleic acids. Quantification of nucleic acids. Electrophoresis of nucleic acids.
Restriction enzymes and cloning techniques.
DNA amplification by polymerase chain reaction (PCR). Reverse transcription polymerase chain reaction (RT-PCR) and quantitative PCR. Production of complementary DNA (cDNA).
DNA sequencing.
Plasmid vectors for gene cloning and expression.
Strategies for the expression of recombinant proteins. Production of recombinant proteins as native proteins, inclusion bodies and fusion proteins. Site directed mutagenesis.
Laboratory practice topics
Salting out of proteins using ammonium sulfate precipitation.
Dialysis.
Measurement of protein solutions by Biuret assay.
Ion-exchange chromatography.
Serum proteins electrophoresis.
SDS-PAGE.
Western blotting.
Enzymatic measurement of glucose.
DNA extraction from blood.
PCR
Agarose gel electrophoresis of DNA.
Course Language
Italian
More information
To attend the laboratory practice, students must have completed the on-line training course on Safety and Health in the workplace.
Degrees
Degrees
MEDICINAL CHEMISTRY AND PHARMACEUTICAL TECHNOLOGY
Single-cycle Master’s Degree
5 years
No Results Found
People
People
No Results Found