Exam 4: Protein Structure and Folding
Which of the following is NOT true about protein structure?
B
Compare and contrast the overall shape and function of globular, fibrous, and membrane proteins. Give a specific example of a protein with each type of tertiary structure.
Globular, fibrous, and membrane proteins are three different types of proteins with distinct overall shapes and functions.
Globular proteins are compact, rounded, and water-soluble. They often have a spherical shape and are involved in functions such as enzyme activity, transport, and signaling. An example of a globular protein is hemoglobin, which is responsible for transporting oxygen in the blood.
Fibrous proteins, on the other hand, have a long, extended shape and are often insoluble in water. They are involved in providing structural support and strength to cells and tissues. An example of a fibrous protein is collagen, which is found in connective tissues and provides strength and flexibility to the skin, tendons, and ligaments.
Membrane proteins are embedded within the lipid bilayer of cell membranes and have a variety of functions, including transport of molecules across the membrane, cell signaling, and cell adhesion. An example of a membrane protein is the sodium-potassium pump, which is responsible for maintaining the electrochemical gradient across the cell membrane.
In summary, globular proteins are compact and water-soluble, fibrous proteins are long and provide structural support, and membrane proteins are embedded in cell membranes and have diverse functions related to membrane transport and signaling. Each type of protein plays a crucial role in the overall function and structure of cells and tissues.
You have isolated a novel protein, characterized its structure and determined that it catalyzes the breakdown of a large substrate and has two binding sites. One of these is large, apparently the binding site for the large substrate; the other is small, possibly a binding site for a regulatory molecule. What do these findings suggest to you about the mode of action of this protein?
B
What is meant by primary, secondary, tertiary, and quaternary structures of proteins?
You have just sequenced a new protein found in Tetrahymena and observe that sulfur-containing cysteine residues occur at regular intervals in the sequence. Which hypothesis is supported by this observation?
You are attempting to express a 50 kDa Tetrahymena protein from a cloned gene introduced into E. coli. When you purify the overexpressed protein you find that it is only 25 kDa in size. Discuss possible reasons for this result.
You treat cells with an inhibitor of the 26S proteasome. Predict the effect on cellular protein levels.
Provide an explanation for why you should politely decline a serving of brains at a party hosted by cannibals.
You have determined the amino acid sequence of a new protein. Is it possible to determine the three-dimensional structure of the protein from its sequence? Why or why not?
Describe a specific example of control of enzyme activity by post-translational modification and allosteric regulation.
Replacing an A with a T in a hemoglobin gene is associated with sickle-cell anemia in humans.
Normal: 5′-ATGGTGCACCTGACTCCTGAGGAGAAGTCT-3′
Sickle cell: 5′-ATGGTGCACCTGACTCCTGTGGAGAAGTCT-3′
(a) What is the nucleotide sequence of the normal and sickle-cell hemoglobin mRNA?
(b) What is the amino acid sequence in this part of the polypeptide chain, and what is the amino acid replacement that results in sickle-cell hemoglobin?
(c) Why might this amino acid substitution make a difference in protein structure?
Which of the following illustrates quaternary protein structure?
The frequencies with which different codons are used vary significantly between different organisms and between proteins expressed at high or low levels within the same organism. This is referred to as:
Short unstructured regions of a protein that connect secondary structural elements are called
Use a rough diagram to compare the structures of a protein alpha-helix and a beta-pleated sheet. For simplicity, show only the backbone of the polypeptide chain.
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