First cycle
degree courses
Second cycle
degree courses
Single cycle
degree courses
School of Medicine
PHARMACEUTICAL BIOTECHNOLOGIES
Course unit
STRUCTURAL BIOCHEMISTRY
MEP5070480, A.A. 2017/18

Information concerning the students who enrolled in A.Y. 2017/18

Information on the course unit
Degree course Second cycle degree in
PHARMACEUTICAL BIOTECHNOLOGIES
ME2193, Degree course structure A.Y. 2015/16, A.Y. 2017/18
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Number of ECTS credits allocated 6.0
Type of assessment Mark
Course unit English denomination STRUCTURAL BIOCHEMISTRY
Department of reference Department of Pharmaceutical and Pharmacological Sciences
Mandatory attendance
Language of instruction English
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 PATRIZIA POLVERINO DE LAURETO BIO/10

ECTS: details
Type Scientific-Disciplinary Sector Credits allocated
Core courses BIO/10 Biochemistry 6.0

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
Lecture 6.0 48 102.0 No turn

Calendar
Start of activities 02/10/2017
End of activities 19/01/2018

Examination board
Examination board not defined

Syllabus
Prerequisites: There are not prerequisites
Target skills and knowledge: This course aims to provide an understanding of the major concepts in the ambit of protein structure and folding at the molecular level, as well as to show the most useful and modern techniques to determine the structure and dynamics of proteins.
Examination methods: Oral exam.
Assessment criteria: The ability to critically discuss a topic of the course will be evaluated
Course unit contents: The first part of the course covers the study of the chemical and physical properties of amino acids, peptides and proteins. Specific lectures are dedicated to the folding and unfolding of proteins and to the techniques to monitor the protein structure and folding, such as circular dichroism, fluorescence, FT-Infrared spectroscopy and biocrystallography. Topics regarding the interactions responsible for structure and stability of proteins, the mechanisms of molecular recognition and interactions between proteins are also covered. The recently discovered intrinsically disordered proteins and misfolded proteins, responsible of severe diseases, are discussed in detail. The turnover and mechanisms of proteolysis of proteins is also considered. Specific classes of proteins such as membrane proteins and proteins involved into transport are finally analyzed in relation to their structure and dynamics.
Detailed program
1. Protein primary structure
2. Protein secondary structure
3. Protein tertiary structure
4. Concept of fold, domain
5. Protein quaternary structure
6. Chemical bonds and short/long interactions
7. Protein Folding, Unfolding and Misfolding
8. Protein denaturation
9. Natively unfolded proteins
10.Protein-protein interaction and protein complex
11.Membrane protein
12.Transport across membranes, Endocytosis and involved proteins
13.Spectroscopy and determination of protein structure
14.Fluorescence: theory and applications
15.Circular dichroism: theory and applications
16. Infrared spectroscopy: theory and applications
17. X Ray and biocrystallography
18. Plasmon surface resonance
Planned learning activities and teaching methods: The lessons are presented through slides and power point presentations. If available, short movies are presentaed.
Additional notes about suggested reading: The course is based on recent research articles, PPT presentations, but the consultation of texts and specific books is also recommended
Textbooks (and optional supplementary readings)
  • C. Branden and J. Tooze, Introduction to Protein Structure. --: Zanichelli, Bologna, --. Cerca nel catalogo