The aim is to introduce some of the most advanced analytical methodologies today available to study biomolecular systems
Classes
Biosensors
General properties. Biological receptors. Immobilization procedures: physical trapping, covalent interactions. Non specific interactions of biomolecular system with solid surfaces. Optical trasducers: Absorption, luminescence, optical fiber, surface plasmon resonance. Electrochemical trasducers. Piezoelectric trasducers.
Microscopy
Optical microscopy: resolution, numerical aperture, Rayleigh and Sparrow criteria, magnification, depth field, confocal microscopy, fluorescence microscopy.
Electronic microscopy: De Broglie, electron-matter interactions, secondary electrons, backscattered electrons, Auger electrons.
Scanning electron microscopy: secondary and backscattered electron images. Electron sources.
Transmission electron microscopy: image formation.
Probe microscopies: Atomic force microscopy: piezoelectric trasducers, tip and cantilever. Forces involved, operating modes. Applications in the study of biomolecular systems.
Mass Spectrometry
Ionic sources: EI, CI, FD, FAB. SIMS, LD-MS, MALDI, ESI. Mass analyzers: magnetic sector, quadrupole, time-of-flight, ICR-MS, ion trap: Mathieu equation, SIM, tandem mass spectrometry. Ion generation in MALDI sources. Hyphenated methods. Analysis of protein. Peptide mass mapping and algorithms. Protein sequencing.
-Notes.
-Skoog, Holler, Nieman, “Principles of Instrumental Analysis”, Saunders College publishing.
-Papers the professor will provide