Ateneo - UPO

The contents of the course include the theoretical principles of protein science and any applicative implications and can be summarized as follows: i) fundamental principles and basic notions of protein biochemistry and protein engineering; i) physico-chemical methods for the analysis of protein-protein and protein-ligand interactions with a module dedicated to nuclear magnetic resonance (NMR) techniques; ii) elements of structural biology and associated investigative techniques (X-ray crystallography, cryo-electron microscopy and NMR).

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The course aims to provide the student with an in-depth study of the fundamentals of protein biochemistry with particular attention to the structure-function relationships of biological macromolecules, structural biology and biophysical methods for protein characterization including NMR spectroscopy techniques applied to biomolecules.

Basic knowledge of chemistry, organic chemistry, physics, physical chemistry and biochemistry of proteins.

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Students with physical disabilities, Learning Disabilities or Special Education Needs can request specific services and tools via the Staff Sviluppo e Coordinamento Carriere e Servizi alle Studentesse e agli

Studenti, consulting the University webpage: https://www.uniupo.it/en/services/services- students-physical-or-learning-disabilities

Students with disabilities, learning disabilities or special education needs, once they have contacted the University Staff, can refer to the tutor in charge of the course to define the examination modalities, concerning academic aspects.

The exam will consist of an oral exam for the protein science module and a written exam for the biomolecular NMR module. The final grade will be assigned by the examining commission.

For the protein science module the questions will aim at evaluating the student's preparation in describing the basic theoretical concepts of the technologies presented during the course and in understanding their application potential. Excellence is achieved when the student proves to have a critical knowledge of the concepts presented in the course. For biomolecular NMR the written exam (two hours) consists of: i) n. 2 multiple choice questions on fundamental theoretical aspects; ii) n. 4 open questions about the interpretation of NMR spectra; iii) one spectral problem where the student is asked to work out the chemical structure of a simple organic compound from 1D/2D NMR spectra. A sample exam text will be made available to the students.

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The student must be able to argue and discuss the basic principles relating to the reactivity of biological macromolecules and the structure-function relationship of proteins. They will also have to know the reference techniques for the biochemical and structural characterization of biological macromolecules and their interactions, developing communication skills and independent judgment on all the topics covered in the course.