since he memorized 15, he has only 10 left. so it should be 10/25
The answer is; SET B
Polar molecules interact well with water because there are charged. Water molecules are partially charged (the oxygen end is partially negative while the hydrogen end is partially positive). Therefore polar molecules can interact stably with charged molecules. The hydrophobic end is non-polar and is ‘water-hating’. When mixed with water, the non-polar region clumps up into globules so they don’t interact with water.
Closely related but different, distantly related but similar
Answer:
<u><em>All of the above.</em></u>
Explanation:
1. Their watertight skin minimizes moistures loss: <em>Reptiles have a reputation that they are “slimy” when we touch and hold them; however, they have dry skin, which has even fewer glands than mammals or amphibians. The main special feature of their skin is that the epidermis is heavily keratinized with a layer, which also prevents water loss.</em>
2. Amphibians must lay eggs in water or in moist soil to reduce moisture loss: <em>Because amphibian eggs don't have an amnion, the eggs would dry out if they were laid on the land, so amphibians lay their eggs in water.</em>
3. Reptile egg shells are harder than amphibians' eggs: <em>Reptile eggs are coated with a leathery or brittle coating, and the animals that hatch from them are miniature versions of the full-sized animal parent. In contrast, amphibian eggs are transparent and jelly-like. The animals that hatch from them still must go through metamorphosis.</em>
<u><em>Hope this helps you have a better understanding:) !!</em></u>
Answer/Explanation:
(1) a mutation in the coding region, resulting in an inactive protein
To check to see if there is a mutation, you could extract the DNA from the cancer cells and then perform PCR to amplify the gene of interest. You could then perform sanger sequencing and compare the sequence to the normal gene to see if a mutation is present. To test the effect of the mutation, you would want to see if an active protein has been formed.
To see if a normal sized protein has been formed, you could perform a western blot, comparing the protein band to the WT protein band. If the protein is absent or much smaller, it is likely not a functional protein.
(2) epigenetic silencing at the promoter of the gene, resulting in reduced transcription.
To check for changes in the epigenetic landscape of the promoter, you could perform chromatin immunoprecipitation by extracting the chromatin from the tumour cells and using antibodies for different chromatin marks to see what has changed between the normal cells and the tumor cells. E.g. H3K9me3, H3K27me3. You would perform a pull down with the antibody of interest and then PCR for your promoter to specifically look at changes at that gene compared to normal cells. To test DNA methylation, you could perform bisulfite sequencing.
To see how transcription is affected, you could extract RNA from the tumor and normal cells, and compare the levels of RNA between the two samples by qRT-PCR
