Protein Purification Methods Based on Whole Structure: Size and Shape

What is protein purification methods based on whole structure: size and shape: Although the size and shape of proteins can have some influence on solubility properties, the chief method of exploiting these properties is gel-filtration chromatography. In addition, preparative gel electrophoresis makes use of differences in molecular size. Proteins range in size from the smallest classified as proteins rather than polypeptides, around 5000 Da, up to macromolecular complexes of many million daltons. Many proteins in the bioactive state are oligomers of more than one polypeptide, and these can be dissociated, though normally with loss of overall structure. Thus many proteins have two “sizes”: that of the native state, and that (or those) of the polypeptides in the denatured and dissociated state. Gel-filtration procedures normally deal only with native proteins, whereas electrophoretic procedures commonly involve separation of dissociated and denatured polypeptides.


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