Interaction of light and matter, absorption spectroscopies (UV/vis and infrared), Fluorescence, and Circular Dichroism, Protein IR and FTIR spectroscopy
Column Chromatography, Paper Chromatography, Thin layer Chromatography; Liquid chromatography (Ion exchange, gel permeation and affinity chromatography);Gas Chromatography Electrophoresis: Isoelectric Focussing, Gel Electrophoresis, 2D electrophoresis, Protein detection, 2D DIGE, Proteomic Databases & tool.
Properties of crystals and foundations of X-ray diffraction; the phase problem and methods for its solution including isomorphous replacement, molecular replacement, and multiwavelength anomalous dispersion; model building and model refinement; model analysis.
Principles of nuclear magnetic resonance (NMR), multidimensional NMR spectroscopy, including COSY, TOCSY and NOESY experiments, sequential assignments and structural analysis, practical methods and new developments in the field.
Basics, Spectra, Sample Preparation, Mass Spectrometry Ionization Techniques, Mass analyzers,Peptide fragmentation mechanism, Interpretation of Mass Spectra. Various techniques: Ion-trap (Linear & Quadrupole), MALDI-TOF, LC-ESI-TOF, and LC-ESI-MS/MS
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1. J G Webster. “Bioinstrumentation”. John Wiley & Sons Inc, 2004. 2. B Notting. “Methods in Modern Biophysics”. Springer Verlag Berlin Heidelberg New York, 2003. 3. R K Scopes. “Protein Purification Principles and Practice”. 3rd Edition. Spring International, 2004. 4. G G Hames. “Spectroscopy for the Biological Sciences”,John Wiley & Sons Inc. 2005 5. Andrew J. Link, J Labaer. “Proteomics”. Cold Spring Harbor Laboratory Course Manual, 2009.