Proteins are separated by their molecular weight on SDS-PAGE by the electric current applied. However, the natural charge of proteins is all different. A student ran a native protein gel without SDS. Once gel run was finished, the student used the standard Western blot procedures and buffers that contain SDS to transfer the proteins to membrane. Do you know whether the proteins are separated based on their inherent charge difference or their size (polypeptide chain length)? Please give your reasons.

pur-new-sol

Related Questions