Practicing Success
Practicing Success
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Protein found in a biological system with a unique three-dimensional structure and biological activity is called a native protein. When a protein in its native form, is subjected to physical change like change in temperature or chemical change like change in pH, the hydrogen bonds are disturbed. Due to this, globules unfold and helix get uncoiled and protein loses its biological activity. This is called denaturation of protein. During denaturation secondary and tertiary structures are destroyed but primary structure remains intact. The coagulation of egg white on boiling is a common example of denaturation. |
| Which of the following is a function of chaperone protein? |
It degrades proteins that have folded properly It rescues proteins that have folded improperly and allows them to refold properly It provide a template for how the proteins should fold It degrades proteins that have folded improperly |
| It rescues proteins that have folded improperly and allows them to refold properly |
| Molecular chaperons are proteins that interact with partially folded polypeptides, facilitating correct folding pathways in which folding can occur. |
