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How many bands would a heterotrimer run on native PAGE and reducing SDS-PAGE produce?
How many bands would a homotetramer produce if run on Native PAGE and SDS-PAGE? (Note: assume that the types of interaction between subunits are the same)
A homotrimer comprised of 25 kDa subunits held together by non-covalent bonds and a homodimer comprised of 15 kDa subunits held together by disulfide bonds is run on non-reducing SDS-PAGE. Which of the following proteins is present in the gel and will move the fastest through the gel?
A monomeric protein comprised of 5,670 amino acids would have an approximate weight of:
Three monomeric proteins of equal weight were run on native PAGE. If one of the proteins migrated further than the rest this indicates this protein is:
A homotrimer comprised of 420 amino acid monomers would have an approximate weight of:
A heterodimer is run through a native gel and SDS-PAGE under reducing conditions. In the native gel there is a single band at the 121 kDa band mark. In the SDS-PAGE gel there are two bands one of which is at the 90 kDa mark. Given the following information the smallest subunit of the heterodimer contains approximately: