Menù principale
B016928 - BIOMOLECULE STRUCTURE
Main information
Teaching Language
Course Content
Suggested readings
Learning Objectives
Prerequisites
Teaching Methods
Type of Assessment
Course program
Academic Year 2020-21
Course year
Second year - Second Semester
Belonging Department
Experimantal and Clinical Medicine
Course Type
Single education field course
Scientific Area
CHIM/03 - GENERAL AND INORGANIC CHEMISTRY
Credits
6
Teaching Hours
48
Teaching Term
01/03/2021 ⇒ 11/06/2021
Attendance required
No
Type of Evaluation
Final Grade
Course Content
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Course program
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Lectureship
Teaching Language
Italian
Course Content
AREA OF TEACHING
Biotechnology with chemical and pharmaceutical applications
EDUCATIONAL GOALS
Knowledge and comprehension: primary and secondary structures of proteins. Characterization and comparison of the sequences and 3D structures of proteins. Interaction between proteins and other molecules and ions. Dynamic properties of proteins
Ability to apply: Viewing, analysis and comparison of sequences and protein structures. Modelling the structure of proteins and mutants
Biotechnology with chemical and pharmaceutical applications
EDUCATIONAL GOALS
Knowledge and comprehension: primary and secondary structures of proteins. Characterization and comparison of the sequences and 3D structures of proteins. Interaction between proteins and other molecules and ions. Dynamic properties of proteins
Ability to apply: Viewing, analysis and comparison of sequences and protein structures. Modelling the structure of proteins and mutants
Suggested readings (Search our library's catalogue)
Introduction to Proteins - Structure, Function, and Motion. Amit Kessel, Nir Ben-Tal
Struttura e funzione delle proteine. Gregory A. Petsko, Dagmar Ringe
Proteins : structures and molecular properties. Thomas E. Creighton
Introduzione alla bioinformatica. G. Valle, M. Helmer Citterich, M. Attimonelli, G. Pesole.
Understanding bioinformatics. Marketa Zvelebil, Jeremy O. Baum
Struttura e funzione delle proteine. Gregory A. Petsko, Dagmar Ringe
Proteins : structures and molecular properties. Thomas E. Creighton
Introduzione alla bioinformatica. G. Valle, M. Helmer Citterich, M. Attimonelli, G. Pesole.
Understanding bioinformatics. Marketa Zvelebil, Jeremy O. Baum
Learning Objectives
Knowledge and comprehension: knowledge of the properties of the amino acids and their organization in primary and secondary structures. Knowledge of the methods of characterization and comparison of secondary and tertiary structures of proteins. Understanding of the interaction modes and the associated properties in the recognition between proteins and other molecules or ions. Understanding of the dynamic properties of proteins
Applying knowledge: ability to compare amino acid sequences. Use of programs for viewing, analyzing and comparing protein structures. Ability to model the 3D structure of proteins and their mutants. Ability to evaluate the experimental results of basic structural techniques.
Applying knowledge: ability to compare amino acid sequences. Use of programs for viewing, analyzing and comparing protein structures. Ability to model the 3D structure of proteins and their mutants. Ability to evaluate the experimental results of basic structural techniques.
Prerequisites
Organic Chemistry
Teaching Methods
Frontal instruction. Individual classroom exercises. Demonstrations.
Type of Assessment
Oral exams, at least 8 sessions per year
Course program
What is structural biology. Relevant databases. The aminoacids and the peptide bond. Secondary structure elements of proteins. Dihedral angles and the Ramachandran plot. Tertiary structure. Basics of NMR spectroscopy and X-ray diffraction for the determination of the three-dimensional structure of the macromolecules. Structural motifs and structural domains. The Protein Data Bank. Structural classification of proteins: CATH and SCOP. Dihedral angles and secondary structure of nucleic acids. Methods for comparing protein sequences. Sequence domains. Structural comparison between proteins. Methods for the prediction of protein structure. Methods for the experimental characterization of the secondary structure. Intermolecular interactions involving proteins. The interaction between proteins and metal ions. Cofactors containing metal ions. Zinc-proteins. Iron-proteins. The flexibility of proteins: force field and molecular dynamics. Membrane proteins.