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B021418 - MAGNETIC RESONANCE IN BIOLOGY
Main information
Course Content
Suggested readings
Learning Objectives
Prerequisites
Teaching Methods
Further information
Type of Assessment
Course program
Academic Year 2020-21
Course year
Third year - Annualità singola
Belonging Department
Experimantal and Clinical Medicine
Course Type
Single education field course
Scientific Area
-
Credits
3
Teaching Hours
24
Teaching Term
28/09/2020 ⇒ 11/06/2021
Attendance required
No
Type of Evaluation
Giudizio Finale
Course Content
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Course program
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Lectureship
Course Content
Basic concepts in Magnetic Resonance. Laboratory of NMR Spectroscopy: hands on, practicals and supervised works. Applications of Magnetic Resonance in Structural Biology, metabolomics, diagnostics, drug screening and drug desing, protein-protein interactions.
Isotope labeling techniques and protein preparation.
Isotope labeling techniques and protein preparation.
Suggested readings (Search our library's catalogue)
Learning Objectives
The course aims at providing the students with knowledge and understanding of Magnetic Resonance basic principles, in order to allow students to analyze possibilities and limitations of magnetic resonance in terms for spectroscopic, structural, analytic and diagnostic applications.
The applications presented throughout the course allow the students to make their own judgements on the state of the art in the application and perspectives of Magnetic Resonance in the various fields, with the aim to enable students to evaluate the possible application of MR in their own field of interest/research and to apply their acquired knowledges to design their own scenarios where MR could have a strategic role.
The applications presented throughout the course allow the students to make their own judgements on the state of the art in the application and perspectives of Magnetic Resonance in the various fields, with the aim to enable students to evaluate the possible application of MR in their own field of interest/research and to apply their acquired knowledges to design their own scenarios where MR could have a strategic role.
Prerequisites
Teaching Methods
Further information
Type of Assessment
Dates of examinations are available at: https://sol.unifi.it/docprenot/docprenot
6-8 sessions per year. Examination will consist in a oral colloquium of about 20-30 minutes.
Topics and Aims of the oral colloquium: -Assessment of the acquired base knowledge of magnetic resonance principles; -Discussion on possible application to different aspects of contemporary biology.
6-8 sessions per year. Examination will consist in a oral colloquium of about 20-30 minutes.
Topics and Aims of the oral colloquium: -Assessment of the acquired base knowledge of magnetic resonance principles; -Discussion on possible application to different aspects of contemporary biology.
Course program
Basics principles of Magnetic Resonance spectroscopy. Chemical shift. The protein case: 13C and secondary structure predictions. Biological Magnetic Resonance Data banks. Scalar Couplings, Dipolar Couplings, Nuclear Relaxation. Multidimensional NMR spectroscopy.
The wet lab: preparation of biological samples, uniform and selective isotopic labelings. NMR in structural biology: solution structures via NMR, conformational dynamics and structural dynamics of proteins.
Metalloproteins. Biology of metal cofactors in proteins and transient metal sites. Protein –ligand interaction. In vitro screening. Drug desing. Case studies in inorganic structural biology: Matrix MEtalloproteinases, Iron-Sulfur Proteins, heme proteins.
The Omic world: from genomics to foodomics: metabolomics and its applications.
Imaging: Basic principles of Magnetic Resonance Imaging: spatial localitazion: frequency and phase encoding. Constrast agents, nuclear relaxation. T1 and T2 weighted images.
Experiencing a “true” NMR laboratory (CERM):
1.Sample preparation for NMR spectroscopy, how to record and analyze a 1D spectrum. Characterization and assignment of a test molecule. 2. Structure determination: from sequence specific assignment to distance geometry calculations. 3. Metabolomics in action: sample preparation, running experiments in automated mode, hands on statistical analysis.
The wet lab: preparation of biological samples, uniform and selective isotopic labelings. NMR in structural biology: solution structures via NMR, conformational dynamics and structural dynamics of proteins.
Metalloproteins. Biology of metal cofactors in proteins and transient metal sites. Protein –ligand interaction. In vitro screening. Drug desing. Case studies in inorganic structural biology: Matrix MEtalloproteinases, Iron-Sulfur Proteins, heme proteins.
The Omic world: from genomics to foodomics: metabolomics and its applications.
Imaging: Basic principles of Magnetic Resonance Imaging: spatial localitazion: frequency and phase encoding. Constrast agents, nuclear relaxation. T1 and T2 weighted images.
Experiencing a “true” NMR laboratory (CERM):
1.Sample preparation for NMR spectroscopy, how to record and analyze a 1D spectrum. Characterization and assignment of a test molecule. 2. Structure determination: from sequence specific assignment to distance geometry calculations. 3. Metabolomics in action: sample preparation, running experiments in automated mode, hands on statistical analysis.