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. Polypeptides are synthesized from amino acid building blocks. The condensation reactio between two amino acids to form a dipeptide involves the loss of A) a water molecule. B) an amino group. C) a carbon atom. D) a carboxylic acid group.

. Polypeptides are synthesized from amino acid building blocks. The condensation reactio between two amino acids to form a dipeptide involves the loss of A) a water molecule. B) an amino group. C) a carbon atom. D) a carboxylic acid group.

Anatomy & Physiology
Anatomy & Physiology
1st Edition
ISBN:9781938168130
Author:Kelly A. Young, James A. Wise, Peter DeSaix, Dean H. Kruse, Brandon Poe, Eddie Johnson, Jody E. Johnson, Oksana Korol, J. Gordon Betts, Mark Womble
Publisher:Kelly A. Young, James A. Wise, Peter DeSaix, Dean H. Kruse, Brandon Poe, Eddie Johnson, Jody E. Johnson, Oksana Korol, J. Gordon Betts, Mark Womble
Chapter2: The Chemical Level Of Organization
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68. Polypeptides are synthesized from amino acid building blocks. The condensation reaction between two amino acids to form a dipeptide involves the loss of A) a water molecule. B) an amino group. C) a carbon atom. D) a carboxylic acid group. 69. The variations in the physical characteristics between different proteins are influenced by the overall amino acid compositions, but even more important is the unique amino acid A) number. B) sequence. C) bond. D) orientation. E) size. 70. Protein folding can be studied using a solution of purified protein and a denaturant (urea), a solvent that interferes with noncovalent interactions. Which of the following is observed after the denaturant is removed (e.g., by dialysis) from the protein solution? A) The polypeptide returns to its original conformation. B) The polypeptide remains denatured. C) The polypeptide forms solid aggregates and precipitates out of solution. D) The polypeptide adopts a new, stable conformation. E) None of the above 71. Why is SDS recommended to use in a denaturing polyacrylamide gel for protein analysis? A) SDS may disrupt membrane bilayers if used in a extraction buffer. B) SDS will denature the proteins (i.e., disrupting quaternary and tertiary structure of the proteins), thus linearizing them and facilitating their migration through the gel. C) SDS will confer a uniform negative charge to all proteins in the sample, which then will migrate towards the anode according to their size. D) All of the above E) None of the above
Transcribed Image Text:68. Polypeptides are synthesized from amino acid building blocks. The condensation reaction between two amino acids to form a dipeptide involves the loss of A) a water molecule. B) an amino group. C) a carbon atom. D) a carboxylic acid group. 69. The variations in the physical characteristics between different proteins are influenced by the overall amino acid compositions, but even more important is the unique amino acid A) number. B) sequence. C) bond. D) orientation. E) size. 70. Protein folding can be studied using a solution of purified protein and a denaturant (urea), a solvent that interferes with noncovalent interactions. Which of the following is observed after the denaturant is removed (e.g., by dialysis) from the protein solution? A) The polypeptide returns to its original conformation. B) The polypeptide remains denatured. C) The polypeptide forms solid aggregates and precipitates out of solution. D) The polypeptide adopts a new, stable conformation. E) None of the above 71. Why is SDS recommended to use in a denaturing polyacrylamide gel for protein analysis? A) SDS may disrupt membrane bilayers if used in a extraction buffer. B) SDS will denature the proteins (i.e., disrupting quaternary and tertiary structure of the proteins), thus linearizing them and facilitating their migration through the gel. C) SDS will confer a uniform negative charge to all proteins in the sample, which then will migrate towards the anode according to their size. D) All of the above E) None of the above
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