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

as a dimer consisting of two identical monomers (80 kDa subunits) that are packed together via hydrophobic interactions

Explanation:

SDS-PAGE (sodium dodecyl sulphate–polyacrylamide gel electrophoresis), is an electrophoretic methodology used to separate proteins that have a molecular weight between 5 to 250 kDa. SDS is a well-known ionic detergent that is able to break hydrophobic interactions and hydrogen bonds. Moreover, size-exclusion chromatography is a filtration technique that separates molecules in solution according to their molecular size. In this case, SDS-PAGE showed that the target protein is composed of two identical subunits (monomers) of 80 kDa each, which were separated by the detergent and formed one single band in the SDS-PAGE gel.

answer: i feel like it would be 3

explanation:

wild parsnip is a perennial plant which reproduces rapidly in areas which have no sign of agricultural activity such roadside or at no tillage open areas. it's considered invasive because it can inhibit the growth of another plant  and its reproduction is fast. there are several harmful effects of this invasive plant although its taproot is edible since it is a member of the carrot family. wild parsnips can cause skin blistering when in contact because of the chemicals it contains, second it inhibits the growth of other plants, it will restrict the growth of animals when eaten and lastly, it drives away natural pollinators like bees.