Many protein-protein associations that exist within the cell remain intact when

Question

Many protein-protein associations that exist within the cell remain intact when a cell is lysed under nondenaturing conditions. Thus, if protein X is immunoprecipitated, then protein Y, with stably associated with X, may also precipitate. Coimmunoprecipitation most commonly used to test whether two proteins of interest are associated in vivo, but it can also be used to identify interacting partners of a target protein. In both cases, the cells, labeled with^35S-methionine, are collected and lysed under conditions that preserve protein-protein interactions. The target protein is specifically immunoprecipitated from the cell extracts, and the immunoprecipitates are fractionated by SDS-PAGE. When performing SDS-PAGE, proteins A are separated on the degree of charge differences. B move through the polyacrylamide gel in a state that is predominantly primary structure. C have been denatured by the breaking of covalent bonds. D emit a wavelength 280 nm light that allows for their detection using x-ray film E stay connected with other proteins and small molecules via hydrogen bonding. Allowing for cell growth in the presence of radioactive methionine will result in which one of the following becoming "labelled"? A The methionine tRNA gene. B The oligosaccharides used in N-linked glycosylation C Phospholipids found in the ER membrane D The mRNA's transcribed during the growth period CE The protein calnexin Under the above described conditions, which technique would best be used to detect coimmunoprecipitated proteins? A Southern blot B Autoradiography C Differential centrifugation E D PCR

Explanation / Answer

1) When performing SDS - PAGE,proteins are seperated according to the molecular weight based on thier differential rates. So i think option A is correct because they are seperated on the degree of charge differences.

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