CHAPTER 5 STUDY GUIDE ---The Structure & Function Of Biological Molecules---

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24 Terms

1
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What are the four major classes of macro/biomolecules?

- Carbohydrates

- Lipids

- Proteins

- Nucleic Acids

2
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What is a polymer? A monomer?

- Polymer: macromolecules made of building blocks (monomers)

- Monomer: single parts that make up polymers

3
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Explain how the two are related by the processes of dehydration and hydrolysis.

- Dehydration: monomers join together to form a polymer

- Hydrolysis: a polymer is broken down into monomers

4
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Name the main categories of carbohydrates and how they relate to each other structurally.

- Monosaccharide (simple sugars)

- Disaccharide (double sugars)

- Polysaccharide (many sugars)

5
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Explain how the same type of carbohydrate component can be linked together to form either energy storage products or structural support material, using starch and cellulose as examples.

- Cellulose is the structural material of polysaccharides and it stores starch (in plants.)

- Cellulose: cell wall structure in plants; linear linked chain of glucose by hydrogen bonding.

6
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How do starch, glycogen, and cellulose each differ in structure and function? In what organisms does each occur?

- Cellulose and starch are in plants, while glycogen is energy storage in animals.

7
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Describe the important chemical properties of lipids in relation to their energy content (vs. protein and carbs) and solubility characteristics.

- Lipids: energy-dense energy, hydrophobic molecules that store energy due to their hydrocarbon chains.

- Insoluble in water, requiring emulsification for digestion.

8
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What is a fat (triglyceride) composed of? How do saturated fats and unsaturated fats differ, and how does this explain their physical state at room temperature?

- Triglyceride: made of a glycerol molecule linked to three fatty acids (either saturated or unsaturated fats).

- Saturated fats: straight chains, single bonds; solid at room temp.

- Unsaturated fats: double bonds, spread out, liquid at room temp.

9
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What are steroids using the cholesterol molecule as an example and giving some examples of its modification into specially functioning molecules?

- Steroids: 4 ringed molecule; basis of cholesterol and hormones.

- Cholesterol: made in liver and/or digested. Maintains plasma membrane and starter molecule to make steroid hormones.

- Too much cholesterol leads to hardening of the arteries, heart attacks, and strokes.

10
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What is a phospholipid? What is their main importance in biology? Explain how and why phospholipids form a bilayer in water.

- Phospholipids: phosphate group attaches to glycerol instead of 3rd fatty acid in triglycerides

- Has a polar hydrophilic head and nonpolar hydrophobic tail

- Assembles by self-assembly

11
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What are the building blocks of proteins? How many kinds are there? Where are they similar and where do they differ from each other structurally?

- Made up of a polymer chain of amino acids (also called polypeptides)

- 20 amino acids makes one protein

- All have R-chain that dictates its properties

12
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What is a peptide bond and how does it form?

- Peptide bonds: monomers amino acids chemically linked together between carboxyl g of one AA and amino of another

- Forms through dehydration synthesis

13
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What function can proteins provide?

- Catalyst (speed up chemical reactions), movement, immune system, signaling, structure, transport

14
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Describe what an enzyme is by explaining its structure, and how they work and why they're so important.

- Enzyme: biological catalysts including an active site, and proteins. They sustain metabolism.

15
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Explain what is meant by primary, secondary, tertiary, and quaternary structure of a protein.

- Primary structure: sequence, determined by DNA code

- Secondary structure: H-bonding

- Tertiary structure: disulfide, ionic bonding, hydrophobic core

- Quaternary structure: interaction between 2+ proteins

16
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Why is the three-dimensional shape of a protein so important?

- If enzyme loses its shape it no longer can catalyze its reaction

17
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Explain what denaturation of a protein is and give an example.

- Denaturation: when a protein's specific 3D structure unfolds and changes due to heat, acid, and chemicals causing it to lose its biological function

18
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What are the three components of a nucleotide?

- Pentose sugar, phosphate, nitrogenous base

19
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How are nucleotides linked together to form nucleic acid chains? To which end of the chain are new nucleotides added?

- New nucleotides are always added to the free 3' hydroxyl end of the growing chain, extending it in the 5' to 3' direction

20
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What is DNA?

- DNA: deoxyribonucleic acid, genes that are units of inheritance

21
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How do the purine bases differ from the pyrimidines? Which bases pair with each other, and what kinds of bonds hold them together?

- Pyrimidines: single C & N ring, T & C

- Purines: double C & N ring, A & G

22
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Describe the three-dimensional shape of the DNA molecule and how its components are arranged.

- Double helix, with two sugar-phosphate backbones and paired nitrogenous bases linked by hydrogen bonds. The strands are anti-parallel as they run in opposite directions.

23
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What is RNA?

- RNA: Ribonucleic acid, reads DNA code and allows synthesis of proteins.

24
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In what ways do DNA nucleotides differ from RNA nucleotides?

- DNA has T, C, A, G while RNA includes U instead of T.

- DNA is double helix while RNA is single helix.

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