METODI FISICI IN CHIMICA BIOORGANICA

The course aims to provide students with a solid theoretical and practical knowledge in the use of IR, UV-Vis and NMR spectroscopic techniques, with particular attention to the analysis of proteins, polymers and complex materials. Through lectures and laboratory experiences, students will acquire the skills needed to interpret and analyze complex spectra, understanding the structural and functional information that can be obtained from each technique.

During the course, students will learn to use infrared spectroscopy for the study of the secondary structure of proteins and for advanced applications such as the analysis of pharmaceutical materials, microplastics and coatings. UV-Vis spectroscopy will allow to characterize the thermal stability of proteins and to interpret the nature of chromophores in organic compounds, while NMR spectroscopy will be used to investigate the dynamics and structure of macromolecules, including proteins and polymers, through multidimensional experiments.

At the end of the course, students will be able to apply spectroscopic techniques to solve complex problems in the chemical and biochemical fields, developing a critical ability in the interpretation of experimental data and in the recognition of molecular structures. They will also be able to use advanced approaches such as saturation difference NMR spectroscopy to study ligand-protein interactions and the investigation of biochemical mechanisms.

Attendance according to the rules of the CdS in CTF http://www.dsf.unict.it/corsi/lm-13_ctf/regolamento-didattico

Module 1: IR Spectroscopy

• Quick review: the basics of IR spectroscopy and why it matters.
• Proteins and IR: how infrared light reveals protein structure and function.
  • IR absorption: protein backbone and amino acid side chains.
  • Advanced techniques: time-resolved IR spectroscopy and differential spectroscopy.
• IR Microscopy: analyzing complex materials.
  • Practical applications: microplastics, coatings, polymers, and food components.
• Hands-on experience: analyzing protein secondary structure using FTIR spectroscopy.

Module 2: UV-Vis Spectroscopy

• The world of absorption: fundamental principles and instrumentation.
  • What are chromophores? How conjugation influences the spectrum.
  • Practical rules (Woodward-Fieser) for interpreting organic compounds.
• Real-world applications:
  • Interpreting UV-Vis spectra in pharmaceuticals and biosciences.
  • Color and thermal stability of proteins.
• Hands-on experience: characterizing protein thermal stability using UV-Vis spectroscopy.

Module 3: NMR Spectroscopy

• Essential review: the principles of NMR spectroscopy.
• Practical insights:
  • Relaxation mechanisms (T1 and T2) and their link to chemical structure.
  • Advanced techniques: Spin-Echo, INEPT, DEPT, and NOESY.
• Dynamic applications:
  • Studying molecular motion and chemical reactions.
  • Analyzing macromolecules: polymers, proteins, DNA, and sugars.
• NMR in medicine:
  • In vivo NMR spectroscopy.
  • Diagnostic applications: magnetic resonance imaging (MRI) and medical spectroscopy.
• Hands-on experience: ligand screening and studying protein-ligand interactions.

1. Horst Friebolin - Basic One and Two-Dimensional N MR Spectroscopy - Wiley
   
2. G. M. Lampman, D. L. Pavia, G. S. Kriz, And J. R. Vyvyan - Introduction to Spectroscopy Fifth edition - CENGAGE Learning.