| The chemicals such as urea and betamercaptoethanol denature proteins. Betamercaptoethanol oxidises disulphide linkages, while urea breaks all the non-covalent bonds found in the native protein molecule. To understand the quaternary structure of a protein, the purified protein was treated with different agents and separated using a gel-filtration column and the following results were obtained: select the incorrect statement. |
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A) The 100 kDa subunit is a homodimer of 50 kDa polypeptide, whereas the 60 kDa subunit is a homotetramer of 15 kDa polypeptide.
B) Disulphide bonds are responsible for multimerisation of 50 and 15 kDa polypeptides into 100 and 60 kDa subunits, respectively.
C) Protein is heteromeric.
D) The protein is a dimer of two polypeptide chains that have relative molecular mass of 100 and 60 kDa each.
Correct Answer: D
Solution :
The native protein is a hexamer - two 50 kDa and four 15 kDa polypeptides.
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