/2100 Resources Hint Submit Answ Hide < Question 14 of 21 > Put the steps of GroEL-GroES chaperonin function in order, starting with an unfolded polypeptide and ending with a polypeptide in its native conformation. Ā© Macmillan Learning Unfolded protein Folded protein Answer Bank ATP is hydrolyzed and the polypeptide, isolated from interfering contact, folds. A GroEL ring binds an unfolded polypeptide and 7 ATP. The GroES "cap" dissociates from the GroEL ring. ADP and the folded polypeptide are released as ATP and GroES bind to the other GroEL ring.
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We need to arrange the provided statements from the "Answer Bank" into the correct sequence. Let's analyze each statement: 1. "ATP is hydrolyzed and the polypeptide, isolated from interfering contact, folds." - This describes a folding event that happens after Show moreā¦
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Which of the following statement about the chaperonin GroEL/S is correct? GroEL/S binds partially folded protein by hydrophilic residues. GroEL/S can fold two proteins at the same time because it is composed of two ring structures. GroEL/S can fold proteins of any sizes. One cycle of protein folding in GroEL/S system requires hydrolysis of seven ATP molecules.
Md.Daniyal A.
Adi S.
3. The important function of molecular chaperones to __________. A. move proteins from endoplasmic reticulum to the Golgi apparatus B. fold proteins into a native conformation C. add cofactors, coenzymes or prosthetic groups to proteins as they are synthesized D. assemble protein subunits into a quaternary structure E. transport proteins to either the plasma membrane or release them from cells to the extracellular space 4. Protein folding to a native conformation is highly dependent upon all of the following, except: A. the rotation about the peptide bond. D. the polar character of sequences of amino acids. B. The relative size of amino acid R-groups E. the rotation about the CĪ±āN bond. C. rotation about the CĪ±āC bond in the backbone.
Dominador T.
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