Biology, 22.02.2020 00:55 hsjsjsjdjjd
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?Interactions of side chains in the protein sequence lead to the formation of a tightly packed core. This core is stabilized by a number of . When a mutation occurs, it destabilizes the protein core and weakens leading to misfolding. a. hydrogen bondsb. polarc. larged. van der Waals contactse. hydrophobicf. disulfide bridgesg. hydrophilich. smalli. nonpolar
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In one or two well-crafted paragraphs in your laboratory journal, summarize the process in which normal cells become cancer cells. your paragraph(s) must include each of the terms listed below. underline each term in your writing:
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In most cases, mutations in the core of a protein that replace a smaller nonpolar side chain in the...
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