The aim of the course is to provide the students with the knowledge of one of the most important methodology in the field of structural biology, namely Nuclear Magnetic Resonance (NMR). NMR can investigate the structure-function correlation of biological macromolecules and deal with the study of complex biological systems. The course, after a short treatment of the basic protein architecture and of the available softwares for visulaisation and analysis of biomolecules, will be substantially dedicated to the investigation of the basic concepts of NMR related to the study of proteins and other biological macromolecules.
Introduction to NMR applied to the study of proteins
basics of the methods
Concept of spin- magnetic moment, precession, larmor frequency,rotating frame, excitation of the signal.
The receiver.
Molecular motions and fluctuating fields.Analysis of motions in proteins
Relaxation measurements: T1 and T2. Nuclear overhauser effect
1D NMR.
Chemical shift
Jcoupling
Scalar and dipolar coupling
2D NMR. COSY, NOESY, TOCSY
Strategies for protein assignment.
Structural restraints- Structure calculations.
3D experiments: isotope labelling
Protein folding
Protein-protein and protein ligand interaction
methoda for the determination of the dissociation constant by NMR
The examination will deal with the presentation and discussion of a paper, dealing with the issues treated during the course, which will be assigned to the student.
******** CSS e script comuni siti DOL - frase 9957 ********p>