Applied Biochemistry
A.Y. 2024/2025
Learning objectives
The course aims to provide students with the theoretical (56 hours of frontal lesson) and practical (16 hours of laboratory practice) basis of the most advanced techniques used in biomedical research and their main applications.
The aim of the course is to provide students with the basic notions for an analytical approach to the different problems encountered in both basic and applied research laboratories.
The training objective of the course is to present and critically discuss biochemical methods to highlight potentiality, limits and complementarity. The contents of the course are constantly updated to train professionals who can fit into a biomedical laboratory with a theoretical preparation suitable for the practical use of the most modern methodologies.
The aim of the course is to provide students with the basic notions for an analytical approach to the different problems encountered in both basic and applied research laboratories.
The training objective of the course is to present and critically discuss biochemical methods to highlight potentiality, limits and complementarity. The contents of the course are constantly updated to train professionals who can fit into a biomedical laboratory with a theoretical preparation suitable for the practical use of the most modern methodologies.
Expected learning outcomes
The students' learning outcomes are assessed by the instructor through a written exam on applied biochemistry based on the course program. The instructor's examination of the students will primarily focus on evaluating the theoretical and practical understanding of biochemical techniques and the skills acquired by the student upon completion of the course. Specifically, the ability to solve typical problems encountered in biochemistry laboratories will be assessed through case study exercises from the literature.
Lesson period: First semester
Assessment methods: Esame
Assessment result: voto verbalizzato in trentesimi
Single course
This course can be attended as a single course.
Course syllabus and organization
Linea AK
Responsible
Lesson period
First semester
Course syllabus
The following topics will be explained during the course:
- UV-Visible Spectrophotometry: Overview of the nature of electromagnetic radiation. UV-VIS spectrophotometry (principles, instrumentation, and applications). Absorption spectra. Lambert-Beer's law and its quantitative applications, the concept of the calibration curve. Spectrophotometric determination of protein concentration. Application of spectrophotometry in enzyme assays.
- Chromatographic Techniques for Purification, Separation, Identification, and Quantitative Analysis of Low (metabolites, drugs, hormones, etc.) and High (nucleic acids and proteins) Molecular Weight Molecules: General principles. Affinity chromatography. HPLC and GC (stationary phases, detectors, and main applications).
- Electrophoretic Techniques: General principles. Gel electrophoresis: agarose, polyacrylamide gel electrophoresis (PAGE and SDS-PAGE). Isoelectric focusing (IEF). Two-dimensional electrophoresis. Detection methods and quantitative evaluations (in-gel staining and post-blotting). Capillary electrophoresis.
- Mass Spectrometry Techniques for Qualitative and Quantitative Analysis of Low (Metabolomics) and High (Proteomics) Molecular Weight Molecules: General principles and instrumentation (sources and analyzers).
- Techniques for Studying Proteins: Methods for sequencing, determining secondary and tertiary structure, post-translational modifications, and mutations.
- Molecular Biology Techniques: Basic concepts of molecular biology. Recombinant DNA (vectors, restriction enzymes, and other enzymes, plasmid DNA purification). Methods for studying transcription and gene expression (mRNA levels, promoter transcriptional activity). Methods for studying macromolecule interactions (DNA-protein, protein-protein). Polymerase chain reaction (PCR) and real-time PCR: principles and applications. Next-generation sequencing (NGS).
- Labeling Methods for Biological Molecules: Overview of types of radioactive decay. Energy and rate of radioactive decay. Detection and measurement of radioactivity. Labeling with non-radioactive systems.
- Cell Cultures and Techniques for Cell Fractionation.
- Immunochemical and Immunometric Techniques: Overview of antibody structure and antigen-antibody reaction. Radioimmunoassays and immunoenzymatic assays.
The course includes mandatory practical laboratory exercises on some of the topics covered in the course.
- UV-Visible Spectrophotometry: Overview of the nature of electromagnetic radiation. UV-VIS spectrophotometry (principles, instrumentation, and applications). Absorption spectra. Lambert-Beer's law and its quantitative applications, the concept of the calibration curve. Spectrophotometric determination of protein concentration. Application of spectrophotometry in enzyme assays.
- Chromatographic Techniques for Purification, Separation, Identification, and Quantitative Analysis of Low (metabolites, drugs, hormones, etc.) and High (nucleic acids and proteins) Molecular Weight Molecules: General principles. Affinity chromatography. HPLC and GC (stationary phases, detectors, and main applications).
- Electrophoretic Techniques: General principles. Gel electrophoresis: agarose, polyacrylamide gel electrophoresis (PAGE and SDS-PAGE). Isoelectric focusing (IEF). Two-dimensional electrophoresis. Detection methods and quantitative evaluations (in-gel staining and post-blotting). Capillary electrophoresis.
- Mass Spectrometry Techniques for Qualitative and Quantitative Analysis of Low (Metabolomics) and High (Proteomics) Molecular Weight Molecules: General principles and instrumentation (sources and analyzers).
- Techniques for Studying Proteins: Methods for sequencing, determining secondary and tertiary structure, post-translational modifications, and mutations.
- Molecular Biology Techniques: Basic concepts of molecular biology. Recombinant DNA (vectors, restriction enzymes, and other enzymes, plasmid DNA purification). Methods for studying transcription and gene expression (mRNA levels, promoter transcriptional activity). Methods for studying macromolecule interactions (DNA-protein, protein-protein). Polymerase chain reaction (PCR) and real-time PCR: principles and applications. Next-generation sequencing (NGS).
- Labeling Methods for Biological Molecules: Overview of types of radioactive decay. Energy and rate of radioactive decay. Detection and measurement of radioactivity. Labeling with non-radioactive systems.
- Cell Cultures and Techniques for Cell Fractionation.
- Immunochemical and Immunometric Techniques: Overview of antibody structure and antigen-antibody reaction. Radioimmunoassays and immunoenzymatic assays.
The course includes mandatory practical laboratory exercises on some of the topics covered in the course.
Prerequisites for admission
To take the exam, students must have passed the Biochemistry and Organic Chemistry I exams.
Teaching methods
The course includes 56 hours of lectures and 16 hours of practical laboratory work. Attendance at the laboratory sessions is mandatory for admission to the exam. During the course, some lessons will be dedicated to solving exam texts.
Teaching Resources
The iconographic material shown during the lessons can be downloaded from the Ariel portal.
In the Ariel portal there is an exercise book that collects the most recent exam themes and the solutions to some problems.
The following texts can be consulted:
Basic Methodologies for Biomolecular Sciences - Reed R, Holmes D, Weyers J, Jones A - Zanichelli ed., last edition.
In the Ariel portal there is an exercise book that collects the most recent exam themes and the solutions to some problems.
The following texts can be consulted:
Basic Methodologies for Biomolecular Sciences - Reed R, Holmes D, Weyers J, Jones A - Zanichelli ed., last edition.
Assessment methods and Criteria
The students' learning outcomes are assessed by the instructor through a written exam on applied biochemistry based on the course program. The written exam consists of two practical exercises and ten multiple-choice questions related to the topics covered in the course. Each practical exercise is worth 10 points, and each multiple-choice question is worth 1 point.
BIO/10 - BIOCHEMISTRY - University credits: 8
Practicals: 16 hours
Lessons: 56 hours
Lessons: 56 hours
Professor:
Ghisletti Serena Maria Luisa
Linea LZ
Responsible
Lesson period
First semester
Course syllabus
The following topics will be explained during the course:
- UV-Visible Spectrophotometry: Overview of the nature of electromagnetic radiation. UV-VIS spectrophotometry (principles, instrumentation, and applications). Absorption spectra. Lambert-Beer's law and its quantitative applications, the concept of the calibration curve. Spectrophotometric determination of protein concentration. Application of spectrophotometry in enzyme assays.
- Chromatographic Techniques for Purification, Separation, Identification, and Quantitative Analysis of Low (metabolites, drugs, hormones, etc.) and High (nucleic acids and proteins) Molecular Weight Molecules: General principles. Affinity chromatography. HPLC and GC (stationary phases, detectors, and main applications).
- Electrophoretic Techniques: General principles. Gel electrophoresis: agarose, polyacrylamide gel electrophoresis (PAGE and SDS-PAGE). Isoelectric focusing (IEF). Two-dimensional electrophoresis. Detection methods and quantitative evaluations (in-gel staining and post-blotting). Capillary electrophoresis.
- Mass Spectrometry Techniques for Qualitative and Quantitative Analysis of Low (Metabolomics) and High (Proteomics) Molecular Weight Molecules: General principles and instrumentation (sources and analyzers).
- Techniques for Studying Proteins: Methods for sequencing, determining secondary and tertiary structure, post-translational modifications, and mutations.
- Molecular Biology Techniques: Basic concepts of molecular biology. Recombinant DNA (vectors, restriction enzymes, and other enzymes, plasmid DNA purification). Methods for studying transcription and gene expression (mRNA levels, promoter transcriptional activity). Methods for studying macromolecule interactions (DNA-protein, protein-protein). Polymerase chain reaction (PCR) and real-time PCR: principles and applications. Next-generation sequencing (NGS).
- Labeling Methods for Biological Molecules: Overview of types of radioactive decay. Energy and rate of radioactive decay. Detection and measurement of radioactivity. Labeling with non-radioactive systems.
- Cell Cultures and Techniques for Cell Fractionation.
- Immunochemical and Immunometric Techniques: Overview of antibody structure and antigen-antibody reaction. Radioimmunoassays and immunoenzymatic assays.
The course includes mandatory practical laboratory exercises on some of the topics covered in the course.
- UV-Visible Spectrophotometry: Overview of the nature of electromagnetic radiation. UV-VIS spectrophotometry (principles, instrumentation, and applications). Absorption spectra. Lambert-Beer's law and its quantitative applications, the concept of the calibration curve. Spectrophotometric determination of protein concentration. Application of spectrophotometry in enzyme assays.
- Chromatographic Techniques for Purification, Separation, Identification, and Quantitative Analysis of Low (metabolites, drugs, hormones, etc.) and High (nucleic acids and proteins) Molecular Weight Molecules: General principles. Affinity chromatography. HPLC and GC (stationary phases, detectors, and main applications).
- Electrophoretic Techniques: General principles. Gel electrophoresis: agarose, polyacrylamide gel electrophoresis (PAGE and SDS-PAGE). Isoelectric focusing (IEF). Two-dimensional electrophoresis. Detection methods and quantitative evaluations (in-gel staining and post-blotting). Capillary electrophoresis.
- Mass Spectrometry Techniques for Qualitative and Quantitative Analysis of Low (Metabolomics) and High (Proteomics) Molecular Weight Molecules: General principles and instrumentation (sources and analyzers).
- Techniques for Studying Proteins: Methods for sequencing, determining secondary and tertiary structure, post-translational modifications, and mutations.
- Molecular Biology Techniques: Basic concepts of molecular biology. Recombinant DNA (vectors, restriction enzymes, and other enzymes, plasmid DNA purification). Methods for studying transcription and gene expression (mRNA levels, promoter transcriptional activity). Methods for studying macromolecule interactions (DNA-protein, protein-protein). Polymerase chain reaction (PCR) and real-time PCR: principles and applications. Next-generation sequencing (NGS).
- Labeling Methods for Biological Molecules: Overview of types of radioactive decay. Energy and rate of radioactive decay. Detection and measurement of radioactivity. Labeling with non-radioactive systems.
- Cell Cultures and Techniques for Cell Fractionation.
- Immunochemical and Immunometric Techniques: Overview of antibody structure and antigen-antibody reaction. Radioimmunoassays and immunoenzymatic assays.
The course includes mandatory practical laboratory exercises on some of the topics covered in the course.
Prerequisites for admission
To take the exam, students must have passed the Biochemistry and Organic Chemistry I exams.
Teaching methods
The course includes 56 hours of lectures and 16 hours of practical laboratory work. Attendance at the laboratory sessions is mandatory for admission to the exam. During the course, some lessons will be dedicated to solving exam texts.
Teaching Resources
The iconographic material shown during the lessons can be downloaded from the Ariel portal.
In the Ariel portal there is an exercise book that collects the most recent exam themes and the solutions to some problems.
The following texts can be consulted:
Basic Methodologies for Biomolecular Sciences - Reed R, Holmes D, Weyers J, Jones A - Zanichelli ed., last edition
Basic Methodologies for Biochemistry and Biotechnology - Ninfa AJ, Ballou DP - Zanichelli ed., last edition.
The principles of biochemistry of Lehninger - Nelson & Cox - Zanichelli ed., last edition.
In the Ariel portal there is an exercise book that collects the most recent exam themes and the solutions to some problems.
The following texts can be consulted:
Basic Methodologies for Biomolecular Sciences - Reed R, Holmes D, Weyers J, Jones A - Zanichelli ed., last edition
Basic Methodologies for Biochemistry and Biotechnology - Ninfa AJ, Ballou DP - Zanichelli ed., last edition.
The principles of biochemistry of Lehninger - Nelson & Cox - Zanichelli ed., last edition.
Assessment methods and Criteria
The students' learning outcomes are assessed by the instructor through a written exam on applied biochemistry based on the course program. The written exam consists of two practical exercises and ten multiple-choice questions related to the topics covered in the course. Each practical exercise is worth 10 points, and each multiple-choice question is worth 1 point.
BIO/10 - BIOCHEMISTRY - University credits: 8
Practicals: 16 hours
Lessons: 56 hours
Lessons: 56 hours
Professor:
Mitro Nico
Shifts:
Turno
Professor:
Mitro NicoEducational website(s)
Professor(s)