Midterm_WI13_Key

7 units in one ring 2 rings back to back any diagram

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7 Units in one ring – 2 rings back to back – Any diagram that will show this will suffice for full points - only diagram with no labeling (1pt) b. Use a diagram to illustrate the folding motif(s) of a single subunit of GroEL (4pts). For full points Apical, Intermediate, and equatorial regions must be clearly identified as well as mention of all the domains containing alpha helices, and the apical domain containing beta sheets. - no labeling (2pt). no labeling, no drawing, and no mention of alpha helices and beta sheets(1pt)
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c. Use a diagram to illustrate the folding motif(s) of a single subunit of the Gro ES complex (4pts). For full points “Roof Beta Hairpin”, “Mobile loop”, and “Beta sheets” must be clearly indicated - no labeling (2pts) -no labeling and no indication of beta sheets in structure(1pt) d. Describe the cycle activity of the GroEL-GroES complex (5pts). Unfolded Protein enters GroEL at side A, 7 ATP bind GroEL at side A (1p), GroES binds at side A, GroES falls off at side B, folded protein falls off at side B, 7 ADP fall off at side B7 ATP are phosphorylated to 7 ADP at side A(1p) and protein folding occurs(1p), 7 ATP bind side B, 7 ADP fall off side A, GroES falls off at side A, folded protein exits at side A (1p), GroEs binds at side B, 7 ATP are hydrolyzed to 7 ADP, protein folding occurs at side B(0.5p). Unfolded protein binds at side A and the cycle starts again(0.5p) e. What is the function of the GroEL-GroES complex (5pts). As the concentrations of misfolded and denatured proteins increase. Due to the numerous solvent-exposed hydrophobic surfaces, these proteins form intermolecular and intramolecular aggregates(1pt). Molecular chaperones such as the GroEl-GroEs complex are proteins which function to reverse these improper associations(2pt) These proteins also assist the folding of non-native polypeptides into
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7 Units in one ring 2 rings back to back Any diagram that...

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