A peptide bond is a covalent bond. This bond is between two amino acid molecules. The formation of a peptide bond occurs when a carboxyl group present on one molecule reacts with an amino group that is present on the molecule. This reaction releases H2O. In organic chemistry, I learned that a sulfide bond has to usually do with C-S-C. A sulfide bond is created by two thiol groups. Below is a picture inserted of both a peptide bond and a sulfide bond.
2. Give an example of the amino acids in a protein that you would expect to form an alpha helix and not a beta pleated sheet. (Name at least 3 different amino acids)
The amino acids that I would expect to …show more content…
Give an example of a transferase and lyase and explain how they differ.
An example of a transferase is peptidyl transderase. An example of lyase is hydroeroxide.Transferases happen when a group of enzymes transfer methyl or possibly glycosyl from one molecule to another. Lyases take place with the joining of two specific molecules by a double bond. A lot of the time you will see this with carbon-carbon bonds.
6. Explain the three steps of translation.
The three steps of translation are initiation, elongation, and termination. The first step which is initiation is when tRNA attaches to an mRNA to start a signal. A complete ribosome is formed and the synthesis is initiated. The next step is elongation and this is when a new tRNA can match the mRNa and link together and the ribosome moves a triplet forward and a new tRNA can enter the ribosome and the procedure is repeated. The third step is termination. This is when the ribosome reaches one of the three stop codons. The release of the polypeptide chain is stimulated in this step (DNA-RNA-Protein). 7. Explain the structural differences between Cytosine, Uracil, and