In most cases, mutations in the core of a protein that replace a smaller nonpola

ID: 149855 • Letter: I

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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?

Reset Help disulfide bridges small van der Waals contacts side chains in the protein sequence lead to the formation of a tightly Interactions of packed When a mutation occurs, it destabilizes the protein core and weakens misfolding core. This core is stabilized by a number of leading to hydrophobic hydrogen bonds hydrophilic polar nonpolar large

Explanation / Answer

Interactions of non polar side chain in the protein sequence lead to the formation of a tightly packed hydrophobic core. This core is stabilized by a large number of hydrogen bonds. When a mutation occurs, it destabilize the protein core and weakens disulfide bridges,leading to misfolding.

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In most cases, mutations in the core of a protein that replace a smaller nonpola

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In most cases, mutations in the core of a protein that replace a smaller nonpola

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