Many purified proteins can maintain their correct folded structure if purified into a solution with the correct pH and salt

Question

Many purified proteins can maintain their correct folded structure if purified into a solution with the correct pH and salt concentrations What would typically happen to a purified protein if a high concentration of urea a molecule capable of disrupting hydrogen bonds is then added to the solution The loss of hydrogen bonds will break the protein up into individual amino acids The protein will become unfolded It could refold if the urea is removed because amino acid sequence alone is sufficient to determine a protein s folded shape The protein will maintain its correctly folded shape because hydrogen bonds are not important for protein folding The protein will become unfolded It won t refold if the urea is removed because proteins require chaperones to determine their correct folded shape

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