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A protein isolated from a thermophilic bacterium shows a molecular weight of 160 kD when eluted from a size-exclusion chromatography column, but when the purified protein is run on an SDS-PAGE gel, a single band of 80 kD is observed. These results tell us that the protein is eluting from the size-exclusion column as a_________(monomer trimer dimer). The SDS-PAGE results allow us to conclude that the protein consists of identical _______(trimers monomers dimers), held together by __________ (hydrophobic hydrophilic hydrogen bonding) interactions which are disrupted by the detergent during the SDS-PAGE procedure.

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luisvaschetto

Answer:

from the size-exclusion column as a dimer...

conclude that the protein consists of identical monomers...

held together by hydrophobic interactions.....

Explanation:

The SDS-PAGE electrophoresis is a common technique used in molecular biology to separate proteins by mass. In this case, a single band of 80 kD is observed because both monomers have an identical molecular weight (i.e., 80 kD + 80 kD = 160 kD). The detergent used in SDS-PAGE (sodium dodecyl sulfate) is able to disrupt hydrophobic interactions such as those involved in protein oligomerization.

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