First cycle
degree courses
Second cycle
degree courses
Single cycle
degree courses
School of Science
CHEMISTRY
Course unit
PROTEIN STRUCTURE AND DYNAMICS
SCP9087646, A.A. 2019/20

Information concerning the students who enrolled in A.Y. 2018/19

Information on the course unit
Degree course Second cycle degree in
CHEMISTRY
SC1169, Degree course structure A.Y. 2018/19, A.Y. 2019/20
N0
bring this page
with you
Degree course track Common track
Number of ECTS credits allocated 6.0
Type of assessment Mark
Course unit English denomination PROTEIN STRUCTURE AND DYNAMICS
Department of reference Department of Chemical Sciences
E-Learning website https://elearning.unipd.it/chimica/course/view.php?idnumber=2019-SC1169-000ZZ-2018-SCP9087646-N0
Mandatory attendance No
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 MASSIMO BELLANDA CHIM/04

ECTS: details
Type Scientific-Disciplinary Sector Credits allocated
Core courses CHIM/06 Organic Chemistry 6.0

Course unit organization
Period First semester
Year 2nd Year
Teaching method frontal

Type of hours Credits Teaching
hours
Hours of
Individual study
Shifts
Lecture 6.0 48 102.0 No turn

Calendar
Start of activities 30/09/2019
End of activities 18/01/2020
Show course schedule 2019/20 Reg.2018 course timetable

Examination board
Examination board not defined

Syllabus
Prerequisites: Basic knowledge of physical-chemistry and biochemistry
Target skills and knowledge: The aim of this course is to provide a basic knowledge of multidimensional NMR, with a practical approach focused on the aspects relevant for the study of structure, dynamics and interactions of macromolecules in solution.
Examination methods: Oral questions with the option to define with the lecturer a specific topic or a case study to discuss at the beginning of the exam.
Assessment criteria: Evaluation will be based on the level of understanding of methodologies covered in the course and on the capabilities shown by the student to interpret them in the context of actual research problems.
Course unit contents: 1. Basic concepts in NMR: introduction to nuclear spin physics, chemical shift, scalar coupling.
2. Relaxation, dipolar coupling, nuclear Overhauser effect (NOE).
3. Practical aspects in the acquisition of NMR spectra: principal components of NMR spectrometer, acquisition and processing of NMR signals, preparation of samples suitable for the NMR analysis.
4. Principle of FT-NMR; Producat Operator formalism to describe NMR experiments.
3. Homonuclear 2D NMR experiments (COSY, TOCSY, NOESY).
6. Heteronuclear correlation spectroscopy: INEPT, HSQC and HMQC experiment.
7. Triple resonance NMR experiments for the study of proteins.
8. Use of NMR data for the structural characterization of peptides and proteins: secondary structure from NMR parameters, high resolution tertiary fold from NOE data. Structure validation.
9. Spin relaxation measurments to evaluate protein dynamics
10.Strategies to study large proteins: TROSY experiments and deuteration.
11. Residual Dipolar Couplings in structural biology.
12. Protein-and protein-ligands interactions by NMR.
13. Production of recombinant labeled proteins.
Planned learning activities and teaching methods: Traditional lessons and short hands-on, cooperative activities.

Lectures will be held in English or Italian depending on the presence of international students or the specific requests of the students enrolled.
Additional notes about suggested reading: Lecture notes and handouts.

The reference books indicated below are available in the library of Department of Chemical Sciences for further reading.
Textbooks (and optional supplementary readings)
  • G.S. Rule and T.K. Hitchens, Foundamentals of Protein NMR Spectroscopy. --: Springer, 2006. Cerca nel catalogo
  • J. Cavanagh,, Protein NMR spectroscopy: principles and practice. --: Elsevier, 2007. 2nd edition Cerca nel catalogo
  • Q. Teng, Structural Biology: Practical NMR Applications. --: Springer, 2005. Cerca nel catalogo
  • J. Keeler, Understanding NMR Spectroscopy. --: John Wiley & Sons, 2010. 2nd edition Cerca nel catalogo
  • T. D. W. Claridge, High-Resolution NMR Techniques in Organic Chemistry. --: Pergamon Press, --. Cerca nel catalogo
  • M.H. Levitt, Spin Dynamics. Basics of Nuclear Magnetic Resonance. --: Wiley, 2003. Cerca nel catalogo

Innovative teaching methods: Teaching and learning strategies
  • Case study
  • Interactive lecturing

Innovative teaching methods: Software or applications used
  • Specific software for the analysis of multidimensional NMR spectra (CARA)

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Quality Education