Applied Biochemistry and Laboratory
A.Y. 2025/2026
Learning objectives
The learning objectives of this course are to:
-Provide students with a comprehensive understanding of the most advanced techniques in biomedical research, encompassing both their theoretical underpinnings (56 lecture hours) and practical applications (16 laboratory hours).
-Develop students' ability to employ an analytical framework for addressing diverse challenges in both fundamental and applied research laboratories.
-Enable students to critically assess biochemical methods, discerning their potential, inherent limitations, and how they can be used in conjunction with one another.
The course content is continuously updated to ensure that graduates are well-prepared, with a strong theoretical foundation, to effectively utilize modern methodologies within a biomedical laboratory environment.
-Provide students with a comprehensive understanding of the most advanced techniques in biomedical research, encompassing both their theoretical underpinnings (56 lecture hours) and practical applications (16 laboratory hours).
-Develop students' ability to employ an analytical framework for addressing diverse challenges in both fundamental and applied research laboratories.
-Enable students to critically assess biochemical methods, discerning their potential, inherent limitations, and how they can be used in conjunction with one another.
The course content is continuously updated to ensure that graduates are well-prepared, with a strong theoretical foundation, to effectively utilize modern methodologies within a biomedical laboratory environment.
Expected learning outcomes
Student learning will be assessed through a written exam on applied biochemistry, covering the course program. The assessment will primarily evaluate students' theoretical and practical understanding of biochemical techniques, as well as their acquired skills. Specifically, their ability to solve typical problems encountered in biochemistry laboratories will be assessed through case study exercises derived from scientific literature.
Lesson period: First semester
Assessment methods: Esame
Assessment result: voto verbalizzato in trentesimi
Single course
This course cannot be attended as a single course. Please check our list of single courses to find the ones available for enrolment.
Course syllabus and organization
Linea AK
Responsible
Lesson period
First semester
Course syllabus
· Cell Culture and Subcellular Fractionation Techniques: Extraction and isolation of proteins and nucleic acids.
· Spectroscopy and Fluorescence:
o UV-Visible Spectrophotometry: Review of the nature of electromagnetic radiation. Principles, instrumentation, and applications of UV-Vis spectrophotometry. Absorption spectra. Beer-Lambert Law and its quantitative applications, including the concept of the calibration curve. Spectrophotometric determination of protein concentration. Application of spectrophotometry in enzyme assays. Quantification of nucleic acids using spectrophotometry and fluorescence.
· Electrophoretic Techniques: General principles. Gel electrophoresis: agarose, polyacrylamide gel electrophoresis (PAGE and SDS-PAGE). Detection methods and quantitative assessments ("in-gel" staining and post-blotting analysis). Capillary electrophoresis.
· 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, transcriptional activity of promoters). Methods for studying macromolecular interactions (DNA-protein, protein-protein). Polymerase Chain Reaction (PCR) and real-time PCR: principles and applications.
· Transfection and Gene Silencing Techniques: (shRNA, siRNA, Cas9 genome editing).
· Next-Generation Sequencing (NGS) Techniques and Applications: Principles of genomics, epigenomics, and transcriptomics.
· Mass Spectrometry Techniques for Qualitative and Quantitative Analysis of Low (Metabolomics) and High (Proteomics) Molecular Weight Molecules: General principles and instrumentation (ion sources and analyzers).
The course includes mandatory practical laboratory exercises covering some of the topics discussed in the lectures.
· Spectroscopy and Fluorescence:
o UV-Visible Spectrophotometry: Review of the nature of electromagnetic radiation. Principles, instrumentation, and applications of UV-Vis spectrophotometry. Absorption spectra. Beer-Lambert Law and its quantitative applications, including the concept of the calibration curve. Spectrophotometric determination of protein concentration. Application of spectrophotometry in enzyme assays. Quantification of nucleic acids using spectrophotometry and fluorescence.
· Electrophoretic Techniques: General principles. Gel electrophoresis: agarose, polyacrylamide gel electrophoresis (PAGE and SDS-PAGE). Detection methods and quantitative assessments ("in-gel" staining and post-blotting analysis). Capillary electrophoresis.
· 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, transcriptional activity of promoters). Methods for studying macromolecular interactions (DNA-protein, protein-protein). Polymerase Chain Reaction (PCR) and real-time PCR: principles and applications.
· Transfection and Gene Silencing Techniques: (shRNA, siRNA, Cas9 genome editing).
· Next-Generation Sequencing (NGS) Techniques and Applications: Principles of genomics, epigenomics, and transcriptomics.
· Mass Spectrometry Techniques for Qualitative and Quantitative Analysis of Low (Metabolomics) and High (Proteomics) Molecular Weight Molecules: General principles and instrumentation (ion sources and analyzers).
The course includes mandatory practical laboratory exercises covering some of the topics discussed in the lectures.
Prerequisites for admission
To be eligible to take the final examination, students must have successfully passed the Biochemistry and Organic Chemistry I exams.
Teaching methods
The course comprises a total of 56 hours of frontal lectures and 16 hours of practical laboratory exercises, conducted at individual workstations. Please note that attendance at laboratory exercises is mandatory and constitutes an essential prerequisite for admission to the final examination.
To foster effective and engaging learning, the didactic approach will integrate innovative methodologies. These include the flipped classroom approach, the use of the interactive Wooclap platform for real-time feedback and active student engagement, and the incorporation of JoVE video resources.
Furthermore, a significant portion of the frontal lectures will be dedicated to the guided resolution of past exam papers, aiming to support students in their preparation and to consolidate acquired competencies.
To foster effective and engaging learning, the didactic approach will integrate innovative methodologies. These include the flipped classroom approach, the use of the interactive Wooclap platform for real-time feedback and active student engagement, and the incorporation of JoVE video resources.
Furthermore, a significant portion of the frontal lectures will be dedicated to the guided resolution of past exam papers, aiming to support students in their preparation and to consolidate acquired competencies.
Teaching Resources
All illustrative material presented during lectures, including lecture slides and associated JoVE videos, can be downloaded from the Ariel portal. Additionally, past exam papers with solutions are available on the Ariel portal.
The following textbooks are recommended for consultation:
· "Metodologie biochimiche e biomelecolari" by Mauro Maccarone - Zanichelli ed., latest edition.
· "Biotecnologie molecolari" by Terry Brown - Zanichelli ed., latest edition.
The following textbooks are recommended for consultation:
· "Metodologie biochimiche e biomelecolari" by Mauro Maccarone - Zanichelli ed., latest edition.
· "Biotecnologie molecolari" by Terry Brown - Zanichelli ed., latest edition.
Assessment methods and Criteria
Student learning outcomes are assessed by the instructor through a written examination covering the applied biochemistry program taught during the course.
The written exam consists of a practical exercise and twenty multiple-choice questions related to the topics covered. The practical exercise is awarded 10 points, and each multiple-choice question is awarded 1 point, for a total of 20 questions.
The written exam consists of a practical exercise and twenty multiple-choice questions related to the topics covered. The practical exercise is awarded 10 points, and each multiple-choice question is awarded 1 point, for a total of 20 questions.
BIO/10 - BIOCHEMISTRY - University credits: 8
Single bench laboratory practical: 16 hours
Lessons: 56 hours
Lessons: 56 hours
Professor:
Ghisletti Serena Maria Luisa
Linea LZ
Responsible
Lesson period
First semester
Course syllabus
· Cell Culture and Subcellular Fractionation Techniques: Extraction and isolation of proteins and nucleic acids.
· Spectroscopy and Fluorescence:
o UV-Visible Spectrophotometry: Review of the nature of electromagnetic radiation. Principles, instrumentation, and applications of UV-Vis spectrophotometry. Absorption spectra. Beer-Lambert Law and its quantitative applications, including the concept of the calibration curve. Spectrophotometric determination of protein concentration. Application of spectrophotometry in enzyme assays. Quantification of nucleic acids using spectrophotometry and fluorescence.
· Electrophoretic Techniques: General principles. Gel electrophoresis: agarose, polyacrylamide gel electrophoresis (PAGE and SDS-PAGE). Detection methods and quantitative assessments ("in-gel" staining and post-blotting analysis). Capillary electrophoresis.
· 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, transcriptional activity of promoters). Methods for studying macromolecular interactions (DNA-protein, protein-protein). Polymerase Chain Reaction (PCR) and real-time PCR: principles and applications.
· Transfection and Gene Silencing Techniques: (shRNA, siRNA, Cas9 genome editing).
· Next-Generation Sequencing (NGS) Techniques and Applications: Principles of genomics, epigenomics, and transcriptomics.
· Mass Spectrometry Techniques for Qualitative and Quantitative Analysis of Low (Metabolomics) and High (Proteomics) Molecular Weight Molecules: General principles and instrumentation (ion sources and analyzers).
The course includes mandatory practical laboratory exercises covering some of the topics discussed in the lectures.
· Spectroscopy and Fluorescence:
o UV-Visible Spectrophotometry: Review of the nature of electromagnetic radiation. Principles, instrumentation, and applications of UV-Vis spectrophotometry. Absorption spectra. Beer-Lambert Law and its quantitative applications, including the concept of the calibration curve. Spectrophotometric determination of protein concentration. Application of spectrophotometry in enzyme assays. Quantification of nucleic acids using spectrophotometry and fluorescence.
· Electrophoretic Techniques: General principles. Gel electrophoresis: agarose, polyacrylamide gel electrophoresis (PAGE and SDS-PAGE). Detection methods and quantitative assessments ("in-gel" staining and post-blotting analysis). Capillary electrophoresis.
· 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, transcriptional activity of promoters). Methods for studying macromolecular interactions (DNA-protein, protein-protein). Polymerase Chain Reaction (PCR) and real-time PCR: principles and applications.
· Transfection and Gene Silencing Techniques: (shRNA, siRNA, Cas9 genome editing).
· Next-Generation Sequencing (NGS) Techniques and Applications: Principles of genomics, epigenomics, and transcriptomics.
· Mass Spectrometry Techniques for Qualitative and Quantitative Analysis of Low (Metabolomics) and High (Proteomics) Molecular Weight Molecules: General principles and instrumentation (ion sources and analyzers).
The course includes mandatory practical laboratory exercises covering some of the topics discussed in the lectures.
Prerequisites for admission
To be eligible to take the final examination, students must have successfully passed the Biochemistry and Organic Chemistry I exams.
Teaching methods
The course comprises a total of 56 hours of frontal lectures and 16 hours of practical laboratory exercises, conducted at individual workstations. Please note that attendance at laboratory exercises is mandatory and constitutes an essential prerequisite for admission to the final examination.
To foster effective and engaging learning, the didactic approach will integrate innovative methodologies. These include the flipped classroom approach, the use of the interactive Wooclap platform for real-time feedback and active student engagement, and the incorporation of JoVE video resources.
Furthermore, a significant portion of the frontal lectures will be dedicated to the guided resolution of past exam papers, aiming to support students in their preparation and to consolidate acquired competencies.
To foster effective and engaging learning, the didactic approach will integrate innovative methodologies. These include the flipped classroom approach, the use of the interactive Wooclap platform for real-time feedback and active student engagement, and the incorporation of JoVE video resources.
Furthermore, a significant portion of the frontal lectures will be dedicated to the guided resolution of past exam papers, aiming to support students in their preparation and to consolidate acquired competencies.
Teaching Resources
All illustrative material presented during lectures, including lecture slides and associated JoVE videos, can be downloaded from the Ariel portal. Additionally, past exam papers with solutions are available on the Ariel portal.
The following textbooks are recommended for consultation:
· "Metodologie biochimiche e biomelecolari" by Mauro Maccarone - Zanichelli ed., latest edition.
· "Biotecnologie molecolari" by Terry Brown - Zanichelli ed., latest edition.
The following textbooks are recommended for consultation:
· "Metodologie biochimiche e biomelecolari" by Mauro Maccarone - Zanichelli ed., latest edition.
· "Biotecnologie molecolari" by Terry Brown - Zanichelli ed., latest edition.
Assessment methods and Criteria
Student learning outcomes are assessed by the instructor through a written examination covering the applied biochemistry program taught during the course.
The written exam consists of a practical exercise and twenty multiple-choice questions related to the topics covered. The practical exercise is awarded 10 points, and each multiple-choice question is awarded 1 point, for a total of 20 questions.
The written exam consists of a practical exercise and twenty multiple-choice questions related to the topics covered. The practical exercise is awarded 10 points, and each multiple-choice question is awarded 1 point, for a total of 20 questions.
BIO/10 - BIOCHEMISTRY - University credits: 8
Single bench laboratory practical: 16 hours
Lessons: 56 hours
Lessons: 56 hours
Professor:
Della Torre Sara
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Professor(s)