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SDS-PAGE normally binds to proteins at a ratio of 1.4 grams of SDS for every gram of protein. Hydrophobic proteins, however, have an particularly difficult time binding to SDS because SDS is polar. Hence they may not be well coated in negative charge and may end up traveling down the gel much more slowly than other proteins. This gives them the appearance of much greater molecular weight.

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Q: What causes a protein to migrate on SDS-page in such a way that it appears to be a protein that is much bigger?
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