Protein Chemistry

Proteomics

• 2-D gel electrophoresis and proteome analysis from gels
• Protein isolation, purification, and characterization from gels
• Informatics by UniProt, PIR, GenEmbl

Peptide Synthesis and Mapping

• Milligram to hundred gram range solid phase, solution phase
• Fully automated and manual approaches
• Peptide libraries
• Peptide modifications: Radiolabel, chromogenic, fluorogenic, stable isotope, non-natural amino acids
• Peptide mapping
  • RP HPLCC
  • MALDITOF/MS
  • LC/ES/MS

Biochemical Analysis

• Chromatographic mapping
• Mass spectral analysis and mapping by MALDI-TOF/MS, ES/MS, or PSD/CID/CAF
• Mass spectral protein sequencing
• 2D-gels
• SDS-Page with and without reduction
• FPLC SEC for apparent mol. Wt.
• Light Scattering for determination of aggregates

Amino Acid Composition

• Quantitative determination of all free occurring amino acids
• Determination of free amino acids
• Unusual amino acids: HyPro, HyLys
• Physiological amino acids
• Solution phase, PVDF membrane, PAGE gel samples

Biophysical Characterization and Ligand Binding

• Protein and ligand binding studies by isothermal titration calorimetry (ITC).
  • Determination the binding constant and stoichiometry of binding between molecules, as well as the molar heat, free energy, and entropy of binding.
• Protein and peptide thermal stability characterization by differential scanning calorimetry (DSC)
  • Thermal stability, determination of melting points, temperature and molar heat of unfolding, interpretations can be made as to the mechanism of unfolding.
• Protein structural analysis by Circular Dichroism, Florescence Spectroscopy, Protein Florescence, Light Scattering Spectroscopy (SEC)

Protein Sequence Analysis

• N-terminal sequence Analysis
  • Automated Edman degradation
  • Solution phase, PVDF, PAGE gel or resin-bound peptide samples
• C-terminal Sequence Analysis
  • Enzymatic degradation using carboxypeptidase Y
  • Five time points for analysis

Recombinant Protein Expression

Antibody Production