
There are many possible answers. A few examples: red blood cell, skin cell, nerve cell, liver cell, bacterial cell, and yeast cell.
Again, there are many possible answers. Examples: water, sugar (glucose), oxygen, CO2, calcium, sodium, starch, fats, iron ions.
The groups are marked in the figure below.
The peptide bond is marked in the figure below.
You can make 202 = 400 dipeptides and 20100 proteins
of 100 amino acids.
Most proteins have more than one hundred amino acids, so there are many
more unique proteins possible.
The molecule Leu-Asp has a Leu at the N-terminus and an Asp at the C-terminus. The reverse is true for Asp-Leu. when the backbone of the dipeptides have the same orientation, the side chains (in the coloured frames) of the two molecules cannot be superimposed. They are therefore different.
The side chains are marked. Lysine is positively charged, glutamate negatively.
No, because they would only work in water with temperatures close to 37°C. The enzymes must be adapted to work at a much wider temperature range. The pH of the water is another problem: pepsin, the protease in your stomach, works best at low pH (between pH 1 and pH 2). That would damage your garments. Another problem is that proteases can also break down (digest) each other. The proteases must therefore be adapted to make them stable enough.
Because of base paring 33% G also means 33% C. 100% - 2 x 33% = 34% remains, which should be divided equally between T and A. We therefore have 17% T and 17% A.
transfer-RNA (tRNA) and ribosomal-RNA (rRNA)
First we transcribe the DNA to mRNA. This gives us:
AUGGUAGGCAAGUACUAG
We then translate it to the peptide: Met-Val-Cys-Lys-Tyr-stop.
Note that we disregard the directionality of transcription and
translation.