is Moving to another question will save this response. uestion 9 Which statement
ID: 143821 • Letter: I
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is Moving to another question will save this response. uestion 9 Which statement does NOT describe a feature of the E. coli GroEL/GroES chaperonin system? O A The conformational changes in GroEUGroES do not require external energy input O B. An unfolded protein binds to the hydrophobic surface of the GroEl chamber O C. Constraining a protein inside the GroEL chamber restricts the conformational space a protein can explore while folding D Constraining a protein inside the GroEL chamber prevents protein aggregation O E All of these function in the process of the GroEL/GroES chaperonin. Moving to another auestion will save this response Type here to searchExplanation / Answer
9. A
GroEL-GroES system require external energy input which is in the form of ATP. The binding of unfolded protein occurs due to the hydrophobic surface found inside the GroEL chamber allowing proper hydrophobic collapse of the protein. These two proteins form a chaperonine complex useful for preventing unfolded or misfolded proteins to aggregate inside a cell during stressed conditions.
20. E.
All the points are necessary for increasing tensile strength of the fibrous protein like collagen or keratin protein. The triple-helical structure of collagen is due to mainly three amino acids: glycine, proline, and hydroxyproline. These make up the motif Gly-Pro-X, where X can be any amino acid. In collagen the peptidyl- proline linkages stabilize the rigid structure of three-stranded collagen helix. The fixed angle of the peptidyl-proline or peptidyl-hydroxyproline bond enables each polypeptide chain to fold into a helix .
Similarly in alpha keratin disulphide bonds (S-S) made by SH side chains cystines gives tensile strength to the protein. The formation of these disulphide bonds require oxidising environment inside the compartment like endoplasmic reticulum.
21. B.
The structure II is the real life scenario explaining how biomolecules like proteins fold inside the cell from its linear polypeptide chain structure to a biologically functional 3D conformation. In an attempt to fold it forms many intermediate structure till it can achieve the least energy state. There is a hydrophobic collapse followed by side chain interactions and various structures emerge as intermediates due to this until the best stabilty is obtained, so the graph is funnel shaped with peaks of high and troughs of low energy states. Finally the bottom (N) is the most stable structure thermodynamically possible for that protein.
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