Which type of interaction stabilizes the alpha helix and the beta pleated sheet
ID: 99333 • Letter: W
Question
Which type of interaction stabilizes the alpha helix and the beta pleated sheet structures of proteins? A) hydrophobic interactions B) disulfide bonds C) ionic bonds D) hydrogen bonds E) peptide bonds Misfolding of polypeptides is a serious problem in cells. Which of the following diseases are associated with an accumulation of misfolded polypeptides? A) Alzheimer's only B) Parkinson's only C) diabetes mellitus only D) Alzheimer's and Parkinson's only E) Alzheimer's, Parkinson's, and diabetes mellitus Changing a single amino acid in a protein consisting of 325 amino acids would A) alter the primary structure of the protein, but not its tertiary structure or function. B) cause the tertiary structure of the protein to unfold. C) always alter the biological activity or function of the protein. D) always alter the primary structure of the protein and disrupt its biological activity. E) always alter the primary structure of the protein, sometimes alter the tertiary structure of the protein, and affect its biological activity. Which of the following statements is true regarding the molecule illustrated in Figure 5.2? A) It is a saturated fatty acid. B) A diet rich in this molecule may contribute to atherosclerosis. C) Molecules of this type are usually liquid at room temperature. D) It is a saturated fatty acid and a diet rich in this molecule may contribute to atherosclerosis. E) It is a saturated fatty acid, a diet rich in this molecule may contribute to atherosclerosis, and molecules of this type are usually liquid at room temperature.Explanation / Answer
38. Ans- d
a)hydrophobic interaction- The hydrophobic form between water and non-polar molecules like fat that has a long chain of carbons which do not interact with water molecules.
b) disulphide bond- Disulfide bond form between two cysteine amino acids by oxidation process which increases the stability of a protein.
c) ionic bond- ionic bonds form between negatively and positively charged side-chain groups of amino acid that stabilize the tertiary structure of a protein.
d)hydrogen bond –the a-helix and b sheet are stabilized by H-bond that form between amino and carbonyl groups.
e) peptide bond- Peptide bonds form between two amino acids in which the carboxyl group of one molecule reacts with the amino group of the other molecule.
39. Ans- d
When protein is folded incorrectly due environmental change or mutation is called protein misfolding. Disease associated with misfolding of protein is Alzheimer's disease, Parkinson's disease, Huntington's disease, Creutzfeldt–Jakob disease, cystic fibrosis, Gaucher's disease.
Diabetes mellitus 1 occurs when the pancreas's do not produce enough insulin and diabetes mellitus 2 is formed when cells fail to respond insulin properly.
40. Ans- e
The correct form of a protein is the most important for its function. If the protein is folded incorrectly that affect the affinity of the protein to its substrate. When a changing a single amino acid in a protein consisting of 325 amino acid that directly affects the primary structure and therefore also affects its biological function because this changing effect it's tertiary structure which is dependent on the amino acid side chains.
41. Ans- d
A diet rich in saturated fatty acid contributed to cardiovascular disease atherosclerosis.
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