BIOC 384 Chapter Notes - Chapter 4: Sodium Dodecyl Sulfate, X-Ray Crystallography, Protein Kinase
14 Jun 2019
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Document Summary
It consists of a hydrophobic region (hydrocarbon tail) and a hydrophilic region (sulfate group). The sds hydrocarbon region permeates the interior of the protein and binds to hydrophobic groups, which reduces the protein to a coil that consists of negatively charged molecules along its length. Since the sds molecule is negatively charged, this becomes the dominant charge of the complex. The number of sds molecules that bind is proportional to the size of the protein. Thus, the charge/mass ratio won"t change with size. Through denaturing the protein solution with heat prior to gel loading, it breaks any covalent bonds between cysteine residues. Molecular mass can be determined from the gel loading allowing a delay in the migration and the negative charge provides an electric field for movement. In solution, provides a collection of structures using soluble proteins, dynamic information. Crystals are required so the protein structures may reflect the packing of crystals.
