Proteins have primary structure. If you are given a method to know which amino acid is at either of the two termini (ends) of a protein, can you connect this information to purity or homogeneity of a protein?
There are several methods provided by several scientists to find out the sequence of amino acids. Frederick Sanger proposed Sanger’s reagent to know the amino acid sequence in a polypeptide chain.
Sanger used 1-fluoro 2, 4 dinitrobenzene (FD NB) to determine insulin structure. FDNB specifically binds with N-terminal amino acid to form a dinitrophenyl (DNP) derivative of peptide. This DNP- derivative peptide can be identified by chromatography. The identified sequence of amino acids shows the homogeneity of a protein molecule.
Yes, if we are given a method to know the sequence of proteins, we can connect this information to the purity of a protein. It is known that an accurate sequence of a certain amino acid is very important for the functioning of a protein. If there is any change in the sequence, it would alter its structure, thereby altering the function. If we are provided with a method to know the sequence of an unknown protein, then using this information, we can determine its structure and compare it with any of the known correct protein sequence. Any change in the sequence can be linked to the purity or homogeneity of a protein.
For example, any one change in the sequence of haemoglobin can alter the normal haemoglobin structure to an abnormal structure that can cause sickle cell anaemia.
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