Nuclear magnetic resonance and imaging (2010/2011)

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Course code
Henriette Molinari
Academic sector
Language of instruction
Teaching is organised as follows:
Activity Credits Period Academic staff Timetable
Teoria 5 I semestre Henriette Molinari
Laboratorio 1 I semestre Henriette Molinari

Lesson timetable

Learning outcomes

The aim of the course is to provide the students with the knowledge of one of the most important methodology in the field of life science, namely Nuclear Magnetic Resonance (NMR) and its application to molecular Imaging. The course will deal with the basic proinciples of NMR and its applications aimed at the investigation, at molecular level, of: i) structure-function correlation of biological macromolecules, ii) protein-protein, protein-small molecule, protein-membrane interactions, iii) mechanism of protein folding, iv) molecular dynamics, v) complex systems “in cell”, vi) in vitro and in vivo imaging techniques


Basic principles of NMR
The NMR spectrometer
Radiofrequency pulses
Molecular motion and relaxation. T1 and T2
NMR parameters: Chemical shift, J coupling, dipolar coupling, NOE
One dimensional NMR
Two-dimensional and multi-dimensional NMR experiments
Sequential assignments of proteins
Structural calculations and structure validation
Protein-ligand, protein-protein, protein membrane interactions via NMR
KD determination
In cell NMR
Basis of Imaging: Introduction, gradients, spatial encoding of the resonance, Image formation, basic pulse schemes, spin-echo, image contrast and weighting (T1, T2, T2* proton density).

Assessment methods and criteria

The examination will deal with the presentation of a paper, suggested by the teacher, and related to the issues treated during the course.