Subsections
[Cr:4, Lc:3, Tt:0, Lb:0]
- Analyses of Macromolecular Composition, Separations-based analyses,
Protein amino acid analysis, Protein N-terminal sequencing, DNA
sequencing, Mass spectrometry-based analyses, Ionization and detection
technologies, Peptide mass fingerprinting and identification, Protein
sequence determination, Disulphide and epitope mapping, Confirmation
of post-translational modifications, Quantitation of relative protein
expression (I-TRAC).
- Analyses of Macromolecular Conformation (and Interactions),
Separations-based analyses, Chromatography – principles and practice,
Gel filtration chromatography, Ion exchange chromatography,
Reverse-phase chromatography, Hydrophobic interaction chromatography,
Affinity chromatography, Chromato-focusing, Electrophoresis –
principles and practice, SDS-PAGE electrophoresis, Native-PAGE and
Ferguson analyses, Isoelectric focusing to determine pI,
Two-dimensional gel electrophoresis, Capillary electrophoresis,
Agarose gel electrophoresis and its variants, Immuno-electrophoresis,
Classical and novel applications, Mass spectrometry-based analyses,
Hydrogen-deuterium amide labeling-accessibility (H-D exchange),
Proteolytic-accessibility, Mass labeling-accessibility,
Spectroscopy-based analyses, Normal and difference UV-visible
absorption spectroscopy, Normal and difference Circular Dichroism (CD)
spectroscopy, Fluorescence spectroscopy, Time-resolved fluorescence
spectroscopy, Fluorescence polarization measurements, Fluroescence
resonance energy transfer (FRET) measurements, FTIR spectroscopy,
Fundamentals of 1-D NMR spectroscopy, Heteronuclear and
multidimensional NMR methods, Electron paramagnetic resonance (EPR)
methods, Fluorescence correlation spectroscopy (FCS),
Calorimetry-based analyses, Differential scanning calorimetry (DSC),
Isothermal titration calorimetry (ITC), Optical measurements-based
analysis, Surface plasmon resonance (SPR), Dynamic light scattering
(DLS) analyses , Microscopy-based analyses, Confocal microscopy –
principles and practice, Fluorescence resonance energy transfer
(FRET), Fluorescence lifetime imaging (FLIM) analysis, Fluorescence
recovery after photobleaching (FRAP) analysis, Near field fluorescence
imaging (SNOM/TIRF), Atomic force microscopy – principles and
practice, Interaction force measurements, Chemical affinity imaging,
Crystallography-based analysis, Structure-determination by molecular
replacement, Structure-determination by multiple anomalous dispersion
(MAD).
- T. G. Cooper, The Tools of Biochemistry, Wiley-Interscience
(1977).
- D. A. Skoog, F. J. Holler and S. R. Crouch, Principles of
Instrumental Analysis, 6th Edn., Brooks Cole (2006).
- M. L. Srivastava, Bioanalytical Techniques, Alpha Science
International Ltd (2007).
