Institute for Biocomputation and Physics of Complex Systems of the University of Zaragoza

1.- UV-Vis absorption spectroscopy

  • Instrumentation and applications
  • Chromophores
  • Determination of concentrations, equilibrium and kinetic parameters, redox potentials...
  • Differential spectroscopy: complex formation
  • Chemical and thermal unfolding of biomolecules
  • Quality control, biotechnology and biomedicine

2.- Circular dichroism spectroscopy (CD)

  • Chromophores in biomolecules
  • CD spectra of biomolecules. Deconvolution
  • Secondary and tertiary structure levels in biomolecules
  • Chemical and thermal unfolding of biomolecules
  • Quality control, biotechnology and biomedicine

3.- Emission spectroscopy

  • Fluorophores in biomolecules. Intrinsic and extrinsic fluorescent probes
  • Fluorescence anysotropy
  • Förster resonance energy transfer (FRET)
  • Fluorescence correlation spectroscopy
  • Single particle fluorescence techniques
  • Fluorescence spectra of biomolecules. Deconvolution
  • Chemical and thermal unfolding of biomolecules
  • Kinetic and thermodynamic binding parameters
  • Fluorescent proteins. Image techniques
  • Quality control, biotechnology and biomedicine

4.- Rapid kinetic techniques in spectroscopy

  • Laser pulse-induced kinetic spectrometry and stooped-flow techniques
  • Kinetic and thermodynamic parameters: conformational equilibrium, binding and reactions

5.- Light scattering

  • Static and dynamic light scattering
  • Hydrodynamic radius, giration radius, molecular mass, polydispersity
  • Molecular aggregates and oligomer assembly
  • Quality control, biotechnology and biomedicine

6.- Differential scanning calorimetry (DSC)

  • Fundamentals of DSC: macromolecular stability, unfolding, enthalpy and heat capacity
  • Two-state and non-two state unfolding models
  • Structural stability indexes for proteins
  • Ligand-induced stabilization effect on macromolecules
  • Quality control, biotechnology and biomedicine

7.- Isothermal titration calorimetry (ITC)

  • Fundamentals of ITC: affinity, enthalpy and stoichiometry of binding
  • Simple and complex interaction models: from single binding site to multiple binding sites
  • Cooperative phenomena: homotropy and heterotropy
  • Allosteric macromolecules: mechanisms and models
  • Quality control, biotechnology and biomedicine

8.- Mass spectrometry

  • Fundamentals of mass spectrometry
  • Tandem mass spectrometry
  • MS spectra interpretation
  • Applications in proteomics and metabolomics
  • Quality control, biotechnology and biomedicine

9.- Surface plasmon resonance (SPR)

  • Fundamentals of SPR: signal and equipment
  • Planning an SPR assay: chips, immobilization strategies and regeneration protocol
  • Applications: interaction specificity, concentration determination, kinetic and thermodynamic binding parameters

10.- Analytical ultracentrifugation (AUC)

  • Sedimentation velocity and equilibrium
  • Hydrodynamic parameters, molecular mass and association of biomolecules
  • Determinatioin of association constants in macromolecular interactions
  • Sample fractionation