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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Biology, 22.06.2019 15:00
Pls me i need this ! each cell has genes activated depending on it's job and what kind of cell it is. it is the presence of that causes the repressor protein to fall off and unblock the gene on the lac operon. if a gene is turned on then it is being an additional circular chromosome found in some bacteria that is used in genetic engineering.
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Biology, 22.06.2019 16:00
Where does oogenesis take place ? seminiferous tubules fallopian tubes ovaries uterus
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Biology, 22.06.2019 17:00
Australopithecus robustus was likely the longest-surviving species of australopithecine in south africa. it had: a. large molars, a big face, and a sagittal crest. b. a large body, large teeth, and a sagittal crest. c. a big brain, big teeth, and a big face. d. a big face, large teeth, and a large body
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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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