Question

In most cases, mutations in the core of a protein that replace a smaller nonpolar side chain in the wild-type (e.g., Ala, Val) with a larger nonpolar side chain (e.g., Leu, Ile, Phe, Trp) in the mutant, result in significant destabilization and misfolding of the mutant. What feature of the protein core explains this observation? Why would such a mutation prevent a protein from folding properly? Match the items in the left column to the appropriate blanks in the sentences on the right.

Answer 1

Step-by-step explanation:

we are required to fill in the blank spaces in the attachment.

protein side chains are non polar. so the first answer is non polar. These side chains are hydrophobic in nature. so the second blank is hydrophobic. Non polar substances are known to have large number of van der waal forces. the third answer is large and the fourth is vanderwaals contact. the protein core destabilizes only when there is a weakening of vanderwaals contact which brings about mutation.

dear user your answer should look like this:

Interactions of non polar side chains in protein sequence lead to the formation of a tightly packed hydrophobic core. This core is stabilized by a large number of vanderwaals contact. When a mutation occurs, it destabilizes the protein core and weakens vanderwaals contact leading to misfolding