Nursing Elites

1. What is the main function of the endoplasmic reticulum (ER) in the cell?

• A. To synthesize and transport proteins and lipids
• B. To package and transport proteins
• C. To break down macromolecules
• D. To store genetic material

Correct answer: A

Rationale: The endoplasmic reticulum (ER) is a network of membranes within the cell that plays a crucial role in protein and lipid synthesis. It consists of two types: rough ER, which is studded with ribosomes and involved in protein synthesis, and smooth ER, which is involved in lipid synthesis and detoxification. The ER's main function is to synthesize proteins and lipids, not just package and transport them. While the ER is involved in transporting these synthesized proteins and lipids to other parts of the cell or outside the cell, its primary role is in their synthesis. Breaking down macromolecules is primarily the function of lysosomes, which are membrane-bound organelles containing enzymes for digestion. Storing genetic material is the function of the nucleus, which houses the cell's DNA. The ER is not involved in storing genetic material.

2. What breaks down into glucose to provide energy?

• A. Lipids
• B. Proteins
• C. Carbohydrates
• D. Nucleic acids

Correct answer: C

Rationale: Carbohydrates are broken down into glucose during digestion, providing energy for cellular processes through glycolysis and cellular respiration. Glucose is a primary source of energy for cells, and its breakdown is essential for powering various cellular activities. Lipids are broken down into fatty acids and glycerol, not glucose. Proteins are broken down into amino acids and are not a direct source of glucose. Nucleic acids are not broken down into glucose for energy production.

3. Which of the following are properties of a liquid?

• A. High atomic attraction
• B. Fixed volume
• C. Low pressure
• D. Takes shape of container

Correct answer: D

Rationale: The correct answer is D: 'Takes shape of container.' Liquids exhibit the property of taking the shape of their container while maintaining a fixed volume. This is due to the ability of liquid particles to flow and move freely within the container. Choices A, B, and C are incorrect. Choice A, 'High atomic attraction,' is not a general property of liquids as the level of attraction between liquid particles can vary. Choice B, 'Fixed volume,' is partially correct as liquids do have a fixed volume, but they do not have a fixed shape. Choice C, 'Low pressure,' is not a defining property of liquids.

4. Which of the following factors does not strengthen a scientific argument?

• A. Lack of bias
• B. Extensive use of qualitative research and data
• C. Able to be reproduced and repeated by others
• D. Withstands the test of time

Correct answer: B

Rationale: The correct answer is B. While qualitative data can provide valuable insights, it does not inherently strengthen a scientific argument to the same extent as quantitative data. Quantitative data is generally more precise, measurable, and easier to verify, making it a stronger basis for scientific arguments. Choices A, C, and D all contribute to strengthening a scientific argument. Lack of bias ensures objectivity and reliability, reproducibility by others validates the findings, and standing the test of time indicates the enduring validity and reliability of the argument.

5. What type of bond connects amino acids to form proteins?

• A. Covalent
• B. Peptide
• C. Ionic
• D. Hydrogen

Correct answer: B

Rationale: The correct answer is 'Peptide'. Peptide bonds are the specific type of bond that connects amino acids together to form proteins. These bonds form through a condensation reaction between the amino group of one amino acid and the carboxyl group of another amino acid, creating a covalent bond. While covalent bonds are involved in the formation of peptide bonds, the direct bond connecting amino acids in proteins is the peptide bond. Ionic bonds involve the attraction between charged particles, and hydrogen bonds are weaker bonds compared to covalent and peptide bonds, playing a different role in protein structure.

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