ChelsM
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The study of viral particles has revealed significant information regarding protein folding. Many proteins hae been shown to often spontaneously fold into their functional structures and give an active viral particle. Yet some are incapable of proper folding on their own. It was shown in 1973, for example, that a certain mutant strain of bacteria GroE could not support the assembly of normal phages. Depending on the phage the head or tail was absent from the functionally complete particle. Further research revealed that the bacterial mutants lacked the genes GroEL and GroES that encode two separate proteins GroEL and GroES. Lack of either protein prevented proper assembly of the particle. Further research has revealed proteins in eukaryotic cells BiP (binding protein) with similar sequence and functional homology to the Gro proteins. These protein families are now termed Molecular Chaperones. Chaperone proteins have been found to play a major role in protein functional assembly.
A) Discuss the significant structural characteristics of this family of functional chaperone proteins (often termed chaperonins). Include in your discussion a possible methodology for their discovery.
B) How does their structure aid in their functional roles? Discuss the protein-protein interactions which are a significant aid in their function.
C) It has since been shown that hundreds of different proteins interact with GroEL-GroES. Discuss how this is possible. (Recall how enzymes function at their active sites, how are these families of proteins different?)
D) Question for educated discussion: Do chaperonins act similar to enzymes in directing the folding of proteins? Defend your answer discussing the molecular basis for your answer.
So, I am supposed to write a 1-2 page essay response to this question utilizing reliable references. I have looked in our textbook and the amount of information is minimal. I tried searching the net and did not find anything specific either. Does anyone know of articles, information, or sites that would help me? Also, in regard to question C, does it have to do with the ability of the active site to change shape?
A) Discuss the significant structural characteristics of this family of functional chaperone proteins (often termed chaperonins). Include in your discussion a possible methodology for their discovery.
B) How does their structure aid in their functional roles? Discuss the protein-protein interactions which are a significant aid in their function.
C) It has since been shown that hundreds of different proteins interact with GroEL-GroES. Discuss how this is possible. (Recall how enzymes function at their active sites, how are these families of proteins different?)
D) Question for educated discussion: Do chaperonins act similar to enzymes in directing the folding of proteins? Defend your answer discussing the molecular basis for your answer.
So, I am supposed to write a 1-2 page essay response to this question utilizing reliable references. I have looked in our textbook and the amount of information is minimal. I tried searching the net and did not find anything specific either. Does anyone know of articles, information, or sites that would help me? Also, in regard to question C, does it have to do with the ability of the active site to change shape?