Two methods that are used for direct protein sequencing is N-terminal amino acid

Question

Two methods that are used for direct protein sequencing is N-terminal amino acid sequencing (e.g. Edman degradation, Sanger's method, or using dansy1 derivatives) followed by chromatography or electrophoresis, and mass spectrometry. There is another method for direct protein sequencing which is an application of a biophysical technique you already know- about. Though never really used for this purpose, it is possible and has been used in the past to concoct and/or complete protein sequences, What is the technique and why is it possible to use this technique to directly sequence proteins? What are the limitations to using this technique for sequencing? When sequencing a protein via N-terminal amino acid sequencing or mass spectrometry, why are a series of proteases used?

Explanation / Answer

a) apart from the above two mention methods, there is another method use for direct sequencing. this method is C-terminal amino acid analysis. This uses carboxypeptidase digestion method. this technique take the confirmation directly from the C-terminal fro identificationa and for obtaining partial sequence information. This technique has very limited methods.

b) series of proteases are used because protease plays important role in in digestion of protein. protein specific proteases is used to digest the high quality protein. various all round proteins are used for the multiple purposes during mass spectometry. The main function for which they are considered are cleavage and digestion.

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