You are being hired to study protein turnover in Drosophila melanogaster. As par
ID: 259754 • Letter: Y
Question
You are being hired to study protein turnover in Drosophila melanogaster. As part of this job, your boss has given you a specialized nutrition formulation containing a fixed amount of isotopically labeled (“heavy”) water. The idea is that this “heavy” water would eventually get metabolized and reprocessed within the Drosophila to produce a heavy intact protein, which is what you are interested in. describe how you would isolate and purify this intact heavy protein. What analytical technique would you use to identify that you have indeed isolated the protein of interest. Explain your answer
Explanation / Answer
Proteins are present in four different structures from the time of their formation until the time they gain the functional status. they are primary, secondary, and tertiary structures. some large proteins exhibit even quaternary structure also.
The tertiary structure is the three-dimensional structure. Water is one of the major contributors of maintaining protein's 3-D structure. Proteins may lose their biological functional activity in the absence of sufficient water.
The protein confirmations that are in need of greater hydration are favored by more active water such as heavy water.
Surface water molecules of the proteins are held together most strongly by the positively charged basic amino acids.
The biological activity of proteins depend on the formation of a 2-D hydrogen bonded network, which spans most of the protein interface.
The intramolecular peptide hydrogen-bonding also contributes the structure and stability to the proteins.
For biological activities to be carried out internal molecular motions in proteins are very much required. These internal molecular motions in proteins are dependent on degree of plasticizing. The degree of plasticizing is determined by the level of hydration. Greater the water, greater the plasticity. internal water enables the proper folding of proteins. Proper protein folding is necessary for proper biological activity.
This internal water is expelled out only upon final squeezing by cooperative interactions.
The hydrogen shell protects the protein from certain irreversi ble denaturing effects. Proteins will have no activity, if the surrounding water is at very low density. The dry proteins become functionally rigid.
Water molecules form an integral part of most protein-protein, protein-DNA, and protein-ligand interactions.
To avoid activity loss protein should not get crystallized. crystallization involves removal of entire water from a biologically active protein.
By the use of carbohydrases, lipases and nucleases all the other three biomolecules can be digested and removed. then proteins can be separated by using some sort of density gradient centrifugation.
from the isolated protein mixture by using SDS-PAGE technique proteins can be separated. from the separated proteins by having done the crystallization of the desired protein.
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