1. An amino acid consists of a carbon atom attached to a hydrogen atom, an amine group, a side group, and a _____________ group.…
RNA: RNA is similar to DNA except that instead of deoxyribose as the sugar, it has ribose. It is single stranded, and instead of thymine, there is uracil. There are 3 forms involved in polypeptide synthesis:mRNA: Messenger RNA carries the genetic code outside the nucleus, into the cytoplasm, where it can be read by ribosomestRNA: Transfer RNA carries the amino acids to the ribosomes to link and form a polypeptide chain. tRNA are shaped like clover leaves; there is a different type for every amino acid. At the bottom of every tRNA molecule is an anti-codon that binds to the codon on the mRNA strand. That is how the amino acid is linked to the codon.…
4. Define the term antigen and state which class of organic molecules make the best antigens, and why?…
The tertiary structure is the folding of the polypeptide chain after it has determined its secondary structure. Its shape is due to bonding between the side chains (R groups) (see figure 11), these include;…
1. The primary structure of a protein represents: (*) the amino acid sequence. (2) the functional configuration. (3) the subunits of a protein. (4) a pleated sheet. (5) a alpha helix. 2. In prokaryotes, most genes are organized into operons. One component of an operon is the structural genes. Which of the following best describes a structural gene? (*) a sequence of DNA that specifies a polypeptide. (2) a sequence of DNA that produces tRNA's. (3) a sequence of DNA that interacts with the small ribosomal subunit. (4) a sequence of DNA that is recognized by RNA polymerase. (5) a sequence of DNA that is involved in forming the structure of a double helix molecule. 3. Identify the correct sequence of steps in protein synthesis in prokaryotes: A - binding of large ribosomal subunit to initiation complex B - peptide bond formation C - binding of mRNA to small subunit of ribosome D - binding of charged tRNA to A site E - release of fmet-tRNA and translocation (1) B, C, A, D, E (2) B, E, C, A, D (3) C, E, B, A, D (*) C, A, D, B, E (5) C, D,…
Results from the bending and folding of a polypeptide chain that occurs due to a variety of interactions b/w the amino acid side chains…
5. Adenine, thymine, guanine, cytosine, and uracil are all _N_ __ __ __ __ __ __ __ _B_ __ __ __ __.…
The tertiary structure is the last shape formation that a protein undergoes and is determined by the various interactions that occur involving the variable R-group of each amino acid. This complex three-dimensional structure is stabilized by four forces: hydrogen bonding, hydrophobic bonding, ionic/hydrophilic bonding and disulfide bonding (Borges, 2014).…
15. What is the significance of the start and stop codons? How many of each?…
5. For each of the following four macromolecules, list their i) monomer(s). ii) functional groups. iii) linkage type. iv) primary function. Macromolecules: a) Carbohydrates b) Proteins c) Lipids d) Nucleic acids (Total 8 marks: 1⁄2 mark for each correct answer)…
a. Proteins- macromolecules made of amino acids. Proteins have many functions in the body. Some sources of proteins are whole-grain cereals, dark breads,rice, beans, and meat.…
Proteins are complex molecules that each has a very unique shape, structure and function. The shape of the proteins is held up by a chain of subunits called amino acids that are connected by peptide bonds. Protein structures are formed by four levels of folding. The primary structure is the linear sequence of amino acids. The secondary structure describes the folding of alpha helixes and beta pleated sheets. The tertiary structure represents the overall shape of the protein and the quaternary structure only occurs in a protein consisting of more than one amino acid chain. When the shape, the structure or the function of proteins is incorrect, it is likely because of some type of change in the sequence of the amino acids or whether a certain amino acid required is present.…
In the space below, list the chemicals (above) from the MOST abundant in the human body to the LEAST abundant.…
Another way of which living organisms differ from each other is through proteins. Proteins are made up of amino acids and they condense together to form a dipeptide. Polypeptides are many amino acids bonded together through a peptide bond. The primary structure is the sequence of amino acids in a polypeptide. Each organism has a different sequence of amino acids which make up their base sequence and consequently code their genetics.…
In this practical the acid-base behaviour of amino acids was assessed. Amino acids are amphoteric. They have the basic (amine) and the acidic (carboxylic) functional groups. These show the same type of equilibrium reactions that all weak acids and bases undergo, and the relative amount of each can be altered by adjusting the pH of the solution. For this practical glycine was used as a model to show this unique nature of amino acids. A series of four acid –base titrations were conducted; 25ml of 0.1M glycine in solution titrated against 0.2M NaOH and HCl, and 25ml of 0.1M glycine in formaldehyde titrated against 0.2M NaOH and HCl. The pKa value of glycine was determined. Titrations curves were constructed by reading the pH meter fter every 0.5ml or 1ml addition of titrant.…