Subsections
[Cr:4, Lc:3, Tt:1, Lb:0]
- Introduction to biomolecules/biopolymers- proteins, lipids, carbohydrates, nucleic acids; properties of biopolymers.
- Introduction to fluorescence- Concepts, fundamental physical mechanisms involved in the generation of fluorescence light, interactions between biomolecules and electromagnetic radiation and environmental effects can generate changes in the measured fluorescence parameters, and how these changes can be exploited for monitoring of biomolecules and their interactions.
- Biomolecular Fluorescence Spectroscopy-Foster resonance energy transfer (FRET); Fluorescence lifetime imaging microscopy (FLIM);Fluorescence correlation spectroscopy (FCS); Ultra-sensitive fluorescence spectroscopy; Fluorescence polarization; Stopped Flow fluorescence; Microscopic techniques (fluorescence microscopy, confocal microscopy, total internal fluorescence microscopy).
- Biomolecular Circular Dichroism Spectroscopy- Concepts; Fundamentals of polarization; Differential absorption of light by molecules; Application to bio-molecular structure determination; Application in chemical stability, folding/unfolding kinetics/reactions of proteins, protein-protein interactions, protein-DNA interactions, protein-ligand interactions and DNA-ligand interactions; Stopped flow CD.
- Biomolecular IR Spectroscopy- Concepts; Vibration modes; IR active/inactive modes; IR regions and stretching frequencies; Important stretching frequencies in biology; IR sample preparation; ATR-IR studies; Bio-ATR measurements; 2D IR spectroscopy applied to biomolecules; IR spectroscopy applied to biomedical sciences.
- Biomolecular NMR Spectroscopy- Concepts and fundamentals; Chemical shifts; J-coupling; Assignment of NMR peaks; NMR applied to proteins; Isotope labelling and sample preparation; 2D NMR; Types of 2D NMR and their applications: NOESY, HSQC, COSY, TROSY; Dynamics and Ligand Binding.
- Thermodynamics and Kinetics of Protein folding/unfolding and protein ligand interactionsProtein folding problem; free energy landscape; native and denatured state; the molten globule state; entropy, enthalpy contributions; Gibb’s-Helmholtz equation, van’t Hoff and Arrhenius equations; disulphide bridges, secondary structure formation; multi-domain and multi-subunit proteins; Protein folding inside the cell; chaperones and cellular complexes; protein misfolding, aggregation and diseases.
- Biomolecular Calorimetry: Isothermal Calorimetry, Differential Scanning Calorimetry; Data analysis and applications.
- SPR methods for biomolecular interactions- Concepts and fundamentals; modes; Data analysis and applications.
- Other methods for determining biomolecular interactions- Two-hybrid screening, phage display; co-immunoprecipitation; cross-linking methods; affinity electrophoresis; proximity ligation assay; dynamic light scattering; theoretical methods (docking).
- J. R. Lakowicz, Principles of fluorescence spectroscopy.
- B. Valeur, Molecular fluorescence: Principles and applications.
- J. Cavanagh et al., Protein NMR Spectroscopy - Principles and Practice.
- Charles R. Cantor & Paul R. Schimmel, Biophysical Chemistry (Parts I-III).
- I. Tinoco et al., Physical Chemistry: Principles and Applications in Biological Sciences.
