THREE-DIMENSIONAL MODELING

Course objectives

Understand the main methodologies for determining protein structures. Learn the main methods used in proteomic analysis, the types of data generated, and their key limitations. Determine the thermodynamic stability of proteins and understand their mechanisms of folding. Mechanisms of aggregation and fibrillogenesis. Intermolecular interactions: binding affinity and association/dissociation rate constants. Learn the general principles of the design, heterologous production and mutagenesis of proteins. Acquire capacity of critical reading of scientific papers.

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CARLO TRAVAGLINI ALLOCATELLI Lecturers' profile

Program - Frequency - Exams

Course program
Thermodynamic stability of proteins. Obtaining a denaturation curve by spectroscopic methods at equilibrium. Analysis of a denaturation curve. Protein folding mechanisms. Fast folding kinetics. Characterization of intermediates and transition states. Amyloid fibrils: molecular mechanisms of aggregation and fibrillogenesis. Inter-molecular recognition. Obtaining and analyzing a binding curve at equilibrium. Binding reactions and kinetic experiments. Principles of de novo design of artificial proteins.
Prerequisites
Necessary pre-requisites for a comprehension of the Course are a suitable knowledge of Chemistry (chemical equilibrium, kinetics of chemical reactions), Biology (structure and function of proteins) and Physics (thermodynamics).
Books
Slides, notes and relevant scientific papers discussed during the lessons (available on-line to students on the website of the Course).
Teaching mode
Classroom lessons or online (if required). Laboratory lessons on selected topics, as indicated above in the program and concerning all parts of the study program.
Frequency
Mandatory
Exam mode
The exam will be divided in two parts, corresponding to the two semesters. The minimal overall mark for the exam is 18/30. The written exam includes questions with open answers, as well as multiple choices. The student must show a basic knowledge of biochemistry, structural biology and molecular biology of proteins, together with the capacity to logically connect and apply this knowledge by solving simple experimental problems. If necessary, exams can be administered online.
Lesson mode
Classroom lessons or online (if required). Laboratory lessons on selected topics, as indicated above in the program and concerning all parts of the study program.
  • Academic year2025/2026
  • CourseMedical Biotechnology
  • CurriculumBioingegneristico
  • Year1st year
  • Semester2nd semester
  • SSDBIO/10
  • CFU2