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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.

Human Anatomy & Physiology (11th Edition)
Human Anatomy & Physiology (11th Edition)
11th Edition
ISBN:9780134580999
Author:Elaine N. Marieb, Katja N. Hoehn
Publisher:Elaine N. Marieb, Katja N. Hoehn
Chapter1: The Human Body: An Orientation
Section: Chapter Questions
Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...
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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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