Part A n most cases, mutations in the core of a protein that replace a smaller n

Question

Part A n most cases, mutations in the core of a protein that replace a smaller nonpolar side chain in the wild-type (eg. Ala, Val) with a larger nonpolar side chain (eg., Leu, le, Phe, Trp) in the mutant, result in signiicant destabilzation and misfolding of the mutant What feature of the protein core explains this observation? Why would such a mutation prevent a protein from folding properiy? Match the items in the left column to the appropriate blanks in the sentences on the right Reset disulfide bridges polar nonpolar small large hydrogen bonds side chains in the protein sequence lead to the formation of a tighty packed When mutation occurs, it destabilens the protein core and weakens misfolding core. This core is stablized by a number of leading to van der Waals contacts

Explanation / Answer

Interaction of non polar side chains led to formation of hydrophobic core whuchbus stabilized by large number of disulphide bridges. When mutation occurs, it weakens vanderwaal contacts leading to misfolding.

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