Protein Structure/Function. C483 Spring 2013. 1. Proteins segments which fold first can promote the folding of other sections of the protein into the native conformation by a process known as A ) renaturation . B ) stabilization. C ) hydrophobic interaction.
Download Policy: Content on the Website is provided to you AS IS for your information and personal use and may not be sold / licensed / shared on other websites without getting consent from its author.While downloading, if for some reason you are not able to download a presentation, the publisher may have deleted the file from their server.
C483 Spring 2013
1. Proteins segments which fold first can promote the folding of other sections of the protein into the native conformation by a process known as
C) hydrophobic interaction.
D) disulfide bridge formation.
2. Hydrophobic amino acid sequences in myoglobin are responsible for
A) covalent bonding to the heme prosthetic group.
B) the folding of the polypeptide chain.
C) the irreversible binding of oxygen.
D) A and B above.
3. A hyperbolic binding curve differs from a sigmoidal binding curve in that the hyperbolic curve
A) has a single equilibrium constant for binding.
B) always has a higher dissociate constant than a sigmoidal curve.
C) shows cooperativity.
D) suggests multiple ligand binding.
E) All of the above.
4. Conditions in the tissues which enhance the delivery of oxygen by hemoglobin are the presence of
A) more carbon dioxide present.
B) 2,3 BPG present.
C) lower pH.
D) All of the above.
E) A and B above.
5. True/False The hydrophobic crevice of globin prevents complete electron transfer to the oxygen so that the electron returns to the iron atom when oxygen dissociates.
6. True/False Myoglobin has a greater affinity for oxygen than hemoglobin.
Protein + Molecule of Interest Complex
Ka = [Complex]/[Free Protein][M]
Plot of % bound protein as a function of amount of molecule of interest
Hyperbolic curve for linear scale
Becomes sigmoidal for semi-log scale