#Question id: 12688
#General Aptitude
#Question id: 33337
#Unit 2. Cellular Organization
#Question id: 824
#Unit 1. Molecules and their Interaction Relevant to Biology
why comparisons of the X-ray structures of hyperthermophilic enzymes with their mesophilic counterparts have failed to reveal any striking differences between them?
#Question id: 13007
#Unit 10. Ecological Principles
#Question id: 889
#Unit 1. Molecules and their Interaction Relevant to Biology
The cis and trans GroEL rings undergo conformational changes in a reciprocating fashion, with events in one ring influencing events in the other ring. The entire GroEL/ES chaperonin complex functions as follows;
a) One GroEL ring that has bound 7 ATP also binds an improperly folded substrate protein, which associates with hydrophobic patches that line the inner wall of the GroEL chamber
b) The GroES cap then binds to the GroEL ring like a lid on a pot, inducing a conformational change in the resulting cis ring
c) Within ~10 s the cis ring catalyzes the hydrolysis of its 7 bound ATPs and releases the resulting Pi , which weakens the interactions binding GroES to GroEL
d) A second molecule of improperly folded substrate protein binds to the cis ring, followed by 7 ATP
e) The binding of substrate protein and ATP to the cis ring conformationally induces the trans ring to release its bound GroES, 7 ADP, and the presumably now better-folded substrate protein
Which of the following is incorrect functions of GroEL/ES chaperonin complex?