Pictured below are the structures of several proteins. Answer the following ques
ID: 487669 • Letter: P
Question
Pictured below are the structures of several proteins. Answer the following questions about secondary and tertiary levels of organization. What type of secondary structure dominates in the protein on the left? What molecular forces dominate in this type of secondary structure? (be specific) Same questions as (a) for the protein on the right - note that the top picture is a side view and the bottom is the same protein looking from the top. How are the forces different in protein (a) vs. protein (b)? For this one, describe the various secondary structures in the protein at the right, being as specific as possible. Where is the "hydrophobic core" of the molecule on the right compared to the one of the top left (part -a-)? In spite of its small size, the insulin protein is highly organized. This is probably because of the many disulfide bonds. How do these bonds help organize the structure of this protein? How many chains is insulin made from? Are they the same or different? Describe the quaternary structure of insulin, including disulfide bonding. In solution, two molecules of insulin form a hydrogen bonded pair. What is the new quaternary structure? In the presence of divalent cations, such as Zn^2+ six molecules of insulin form a new, non-water-soluble mass. What is the quaternary structure of this new protein, which is much less clinically useful than the first one?Explanation / Answer
a)the secondary structure present in left protein is alpha helix structure,it consists of single polypeptide chain,it is rod like structure,An alpha helix is especially suited for cross-membrane proteins because all of the amino hydrogen and carbonyl oxygen atoms of the peptide backbone can interact to form intrachain hydrogen bonds while its aliphatic side chains can stabilize in hydrophobic environment of cell membrane.