Part A Inmost cases, mutations ite core of a protein that replace a eaer nonpola

Question

Part A Inmost cases, mutations ite core of a protein that replace a eaer nonpolar side chan n the nedtype te o. Aa v.), awie now ar destablization and misfolding of the mutant What feature of the Match the items in the left column to the appropriate blanks in the sentences on the right the wid-type (e g. Ails Val) with a larger nonpolar side chain (eg. Leu, le. Phe, Trp) in the mutant, result in signiticant protein core expiains this observation? Why would such a mutation prevent a protein from folding properly Reset Help disulfide bridges polar nonpolar small large hydregen bonds hydrophobic van der Waals contacts side chains in the protein sequence lead to the formation ot a sighty core. This core is stablized by a number of packed When a mutation occurs, it destablizes the protein core and weakens misfolding leading to

Explanation / Answer

Interaction of polar side chains of protein sequence leads to formation of a tightly packed hydrophobic core. This core is stabilised by a large number of hydrogen bond. When a mutation occur it destabilizes the protein core and weakens disulphide bridge leading to mis folding.

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