First cycle
degree courses
Second cycle
degree courses
Single cycle
degree courses
School of Science
Course unit
SCP9088062, A.A. 2019/20

Information concerning the students who enrolled in A.Y. 2019/20

Information on the course unit
Degree course Second cycle degree in
SC1731, Degree course structure A.Y. 2014/15, A.Y. 2019/20
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Number of ECTS credits allocated 8.0
Type of assessment Mark
Course unit English denomination ANALYSIS OF BIOMOLECULES
Website of the academic structure
Department of reference Department of Biology
Mandatory attendance
Language of instruction Italian
Single Course unit The Course unit can be attended under the option Single Course unit attendance
Optional Course unit The Course unit can be chosen as Optional Course unit


ECTS: details
Type Scientific-Disciplinary Sector Credits allocated
Core courses CHIM/02 Physical Chemistry 4.0
Core courses CHIM/11 Chemistry and Biotechnology of Fermentations 4.0

Course unit organization
Period First semester
Year 1st Year
Teaching method frontal

Type of hours Credits Teaching
Hours of
Individual study
Laboratory 2.0 32 18.0 No turn
Lecture 6.0 48 102.0 No turn

Start of activities 30/09/2019
End of activities 18/01/2020
Show course schedule 2019/20 Reg.2014 course timetable

Prerequisites: Basics of mathematics, physics and biochemistry.
Target skills and knowledge: The course provides the cultural elements for the investigation of the structure-function relationship in proteins, nucleic acids and their complexes in a molecular approach to the understanding of natural processes. The principal methods for purification and characterization of proteins and conventional and advanced spectroscopic techniques will be considered.
Examination methods: Part A
Written examination with general questions and numerical exercises
Part B
Oral Exam

Evaluation of reports on laboratory experiments
The assessment is weighted on the written/oral exam for 75% and on laboratory reports for 25%. The final mark is the average of the outcomes relating to the two parts, A and B
Assessment criteria: Ability to identify methods of investigation, and use them properly, among those provided as part of the course, to solve any specific problem related to purification and structural-functional characteristics of macromolecules.
Capacity to present, discuss and rationalize data relative to the laboratory experience.
The student will be evaluated based on the level of learning, awareness, ability to reflect and critically discuss the specific skills of the discipline.
Course unit contents: Part A
The course provides the description of biochemical and biophysical techniques used in the study of soluble and membrane proteins, nucleic acids and their complexes, according to the following scheme:
- UV-Vis Absorption Spectroscopy- applications to the study of proteins, cofactors, coenzymes, metalloproteins and nucleotides. Time resolved techniques: applications to the study of enzyme kinetics of electron transfer reactions in proteins and in particular in photosynthesis.
- Techniques using fluorescent probes: fluorescence and fluorescence quenching, fluorescence anisotropy, Energy transfer and FRET (Fluorescence Resonance Energy Transfer), imaging, immunofluorescence; FRAP. Application to biological systems.
- Circular dichroism principles and applications in the field of protein conformation. Determination of protein secondary structure, determination of structural changes induced bu stimulus(for ex. pH, heat, solvent, substrates; studies of folding / unfolding; studies of ligand binding, protein-protein a.d protein-nucleic acids interactions.

Part B
- Introduction to protein purification.
- Principles of chromatographic techniques for proteins: van Deemter equation, efficiency, selectivity and resolution.
- Separation techniques based on macromolecule activity: affinity chromatography (AC).
- Separation techniques based on dimensions: size-exclusion chromatography (SEC).
- Separation techniques based on charges: anion and cation exchange, weak and strong exchangers.
- Separation techniques based on hydrophobicity: hydrophobic interaction and reverse-phase (RP) chromatography.
- Protein stability: conformational stability of proteins; stabilizing interactions in proteins; thermodynamics of the native/denatured transition in proteins.
- Thermodynamic methods for protein characterization: overview of bio-calorimetry (DSC and ITC).
- Hydrodynamic and aggregation properties of proteins in solution: static and dynamic light scattering methods.
- Purification, bio-calorimetry and light scattering applications to proteins.
Planned learning activities and teaching methods: Lectures accompanied by slides
Laboratory experience to be defined each year
Additional notes about suggested reading: Material provided by the teachers: slides, reviews, scientific articles relevant to the topics discussed, laboratory handouts
Textbooks (and optional supplementary readings)
  • Cantor and Schimmel, BIOPHYSICAL CHEMISTRY PartII Techniques for the study of biological structure and function. New York: Freenan and Company, --. Cerca nel catalogo

Innovative teaching methods: Teaching and learning strategies
  • Lecturing
  • Laboratory
  • Problem solving
  • Loading of files and pages (web pages, Moodle, ...)

Innovative teaching methods: Software or applications used
  • Moodle (files, quizzes, workshops, ...)

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