2 An unknown protein sample was subjected to SDSPAGE and yie

2. An unknown protein sample was subjected to SDS-PAGE and yielded one band. When subjected to native PAGE, two bands were observed. Give a reasonable explanation for this behavior. 3. From the lab intro: \"In most cases, SDS binds to proteins in a constant ratio of 1.4 grams of SDS per gram of protein.\" Explain why some proteins do not bind SDS with this ratio. That is, what kinds of proteins give anomalous molecular weights from SDS-PAGE What specific tertiary structure interactions do SDS and mercaptoethanol affect to denature the protein?

Solution

ANSWER FOR QUESTION NO2_In the SDS PAGE ELECTROPHORETIC MOMENT OF PROTEINS IS DEPENDS UPON.THERE MOLECULAR MASS.AND IN NATIVE PAGE IT ELECTROPHORETIC MOMENT DEPENDS UPON PROTEIN CHARGE AND ITS HYDRODYNAMIC SIZE.SO THERE ARE SO MANY POSIBLITIES;THE PROTEIN SAMPLE MAY CONTAIN PROTEINS WITH SIMILAR MOLECULAR WEIGHT BUT WITH DIFFERENT CHARGE.

ANSWER FOR QUETION NO 3-PROTEINS WITH AGRREGATION GIVE ANALOMOUS Molecular weight