First cycle
degree courses
Second cycle
degree courses
Single cycle
degree courses
School of Science
INDUSTRIAL BIOTECHNOLOGY
Course unit
MACROMOLECULAR ANALYSIS
SCN1037554, A.A. 2016/17

Information concerning the students who enrolled in A.Y. 2016/17

Information on the course unit
Degree course Second cycle degree in
INDUSTRIAL BIOTECHNOLOGY
SC1731, Degree course structure A.Y. 2014/15, A.Y. 2016/17
N0
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Number of ECTS credits allocated 8.0
Type of assessment Mark
Course unit English denomination MACROMOLECULAR ANALYSIS
Website of the academic structure http://biotecnologie.scienze.unipd.it/2016/laurea_magistrale
Department of reference Department of Biology
E-Learning website https://elearning.unipd.it/biologia/course/view.php?idnumber=2016-SC1731-000ZZ-2016-SCN1037554-N0
Mandatory attendance
Language of instruction Italian
Branch PADOVA
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

Lecturers
Teacher in charge ROBERTO BATTISTUTTA CHIM/06
Other lecturers DONATELLA CARBONERA CHIM/02

ECTS: details
Type Scientific-Disciplinary Sector Credits allocated
Core courses BIO/10 Biochemistry 4.0
Core courses CHIM/11 Chemistry and Biotechnology of Fermentations 4.0

Mode of delivery (when and how)
Period First semester
Year 1st Year
Teaching method frontal

Organisation of didactics
Type of hours Credits Hours of
teaching
Hours of
Individual study
Shifts
Laboratory 2.0 32 18.0 No turn
Lecture 6.0 48 102.0 No turn

Calendar
Start of activities 01/10/2016
End of activities 20/01/2017

Examination board
Board From To Members of the board
6 ANALISI DI MACROMOLECOLE 2017/2018 01/10/2017 25/11/2018 BATTISTUTTA ROBERTO (Presidente)
CARBONERA DONATELLA (Membro Effettivo)
BELLANDA MASSIMO (Supplente)
5 ANALISI DI MACROMOLECOLE 2016-2017 01/10/2016 30/11/2017 BATTISTUTTA ROBERTO (Presidente)
CARBONERA DONATELLA (Membro Effettivo)
BELLANDA MASSIMO (Supplente)

Syllabus
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
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.
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.
Thermodynamics 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