3 A) The native conformation of a protein is generally the conformation with low
ID: 206893 • Letter: 3
Question
3 A) The native conformation of a protein is generally the conformation with lowest energy, making protein folding an energetically favorable process. Why then are chaperones and chaperonins required to facilitate this folding?
The dense cellular environment favors protein aggregation, which hinders effective protein folding.
Chaperones actively perform protein folding reactions that will not occur spontaneously.
Chaperones are required to form disulfide bonds and other stabilizing covalent bonds between proteins.
Chaperones are needed to create alpha helix and beta sheet structures.
3 B) Which of the following statements about enzymes is FALSE?
The Michaelis constant is an inherent property of an enzyme equal to the substrate concentration that yields maximal reaction rate.
The maximal velocity of an enzymatic reaction is dependent on the concentration of enzyme.
The active site of an enzyme consists of the substrate binding site and the catalytic site.
An enzyme with two distinct substrates for which it has two Km values will have the same maximal reaction velocity.
Explanation / Answer
3A) The proteins after synthesis undergo post translational modifications and attain a naive conformation state. The proteins are capable of attaining naive conformation but require chaperones and chaperonins for proper folding. This because, the proteins after synthe sis undergo aggregation dur to exposure to cellular environments. This aggregation causes destabilization of portein conformation. To prevent this aggrgation and to provide stability, the chaperones and chaperonins assist the proteins attain naive conformation and proper folding. These help for protein folding but are not incorporated into protein structure. option 1 is correct.
3B) Michaelis - Menten equation describes the formation of enzyme - substrate complex as an intermediate in a reaction to increase the rate of reaction. The Km or Michaelis constant is described as substrate concentration equal to half of maximum velocity ( 1/2 Vmax) of a reaction. The Michaelis menten euqation describes chemical reactions with single substate. An enzyme increases the rate of chemical reaction. The active site of enzyme contains substrate binding site and catalytic sites. Therefore, the option 4 is correct.
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