| There are thousands of different proteins in cells, and each protein has a different structure and function. The higher order structure of a protein is the product of its primary, secondary, tertiary, and quaternary structure. Purification and characterization of proteins is essential for elucidating their structure and function. By taking advantage of differences in their size, solubility, charge and ligand binding properties, proteins can be purified to homogeneity using various chromatographic and electrophoretic techniques. The molecular mass and purity of a protein, and its subunit composition, can be determined by SDS-PAGE. The primary structure can be determined by hydrolysis of a protein and automated Edman degradation. Deciphering the primary and three-dimensional structures of a protein by X-ray analysis or nmR spectroscopy leads to an understanding of structure-function relationships in proteins. Mass spectrometry has become a powerful technique for elucidating protein structure, chemical modification, function and homology.
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- Mass spectrometry analysis of blood, urine and tissues is now being applied for clinical diagnosis. Discuss the merits of this technique with respect to specificity, sensitivity, through-put and breadth of analysis, including proteomic analysis for diagnostic purposes.
- Study the role of chaperone proteins in the folding and transport of newly synthesized proteins in the cell.
- Review the importance of protein misfolding and deposition in tissues in age-related chronic diseases.
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| Imai J, Yashiroda H, Maruya M, Yahara I, Tanaka K. Proteasomes and molecular chaperones: cellular machinery responsible for folding and destruction of unfolded proteins. Cell Cycle 2003;2:585-590.
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