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Chapter 5 Reading Quiz. Splitting water. What does “hydrolysis” literally mean? What element composes the backbone of the 4 macromolecules? What subunits come together to make a protein? List the 3 other macromolecules. What is the main function of DNA?. Carbon!. Amino acids.

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Chapter 5 reading quiz
Chapter 5 Reading Quiz

Splitting water

  • What does “hydrolysis” literally mean?

  • What element composes the backbone of the 4 macromolecules?

  • What subunits come together to make a protein?

  • List the 3 other macromolecules.

  • What is the main function of DNA?

Carbon!

Amino acids

Carbohydrates

Lipids

Nucleic acids

information


1 list the four major classes of biomolecules
1.List the four major classes of biomolecules.

  • Carbohydrates

  • Lipids

  • Proteins

  • Nucleic Acids


2 explain how organic polymers contribute to biological unity and diversity
2. Explain how organic polymers contribute to biological unity and diversity.

Unity – there are only 40 – 50 monomers used to make all macromolecules

Diversity – new properties emerge when these monomers are arranged in different ways…leading to the diversity of life 


3 describe how covalent linkages are formed condensation and broken hydrolysis in organic polymers

Condensation unity and diversity.

Polymerization reaction where monomers are covalently linked, removing a water molecule

Remove H2O molecule

Hydrolysis

Reaction process that breaks covalent bonds between monomers by adding water molecules

Add H2O molecule 

3. Describe how covalent linkages are formed (condensation) and broken (hydrolysis) in organic polymers.


4 explain how carbohydrates are classified
4. Explain how carbohydrates are classified. unity and diversity.

Carbohydrates are classified by the number of simple sugars

They are organic molecules made of sugars and their polymers 


5 list four characteristics of sugar
5. unity and diversity.List four characteristics of sugar.

  • An –OH group is attached to each carbon except one, which is =O

    2. The size of the carbon skeleton varies from 3-7 carbons

    3. Spatial arrangement around asymmetric carbons may vary (ex: enantiomers)

    4. In aqueous solutions, many simple sugars form rings. (chemical equilibrium favors ring structures) 


6 identify a glycosidic linkage and describe how it is formed
6. Identify a glycosidic linkage and describe how it is formed.

Glycosidic linkage – the covalent bond formed by a condensation reaction between 2 sugar monomers

Sugar + Sugar  Big Sugar

(monosaccharides) (glycosidic (disaccharide) 

linkage)


7 describe the important biological functions of polysaccharides
7. Describe the important biological functions of polysaccharides.

  • Energy storage – in the form of starch and glycogen

    2. Structural support – in the form of cellulose and chitin 


8 distinguish between the glycosidic linkages found in starch and cellulose

Starch polysaccharides.

Glucose monomers in α configuration

-OH group is BELOW ring’s plane

α 1-4 linkage

Cellulose

Glucose monomers in β configuration

-OH group is ABOVE ring’s plane

β 1-4 linkage 

8. Distinguish between the glycosidic linkages found in starch and cellulose.


9 explain what distinguishes lipids from other major classes of macromolecules
9. polysaccharides.Explain what distinguishes lipids from other major classes of macromolecules.

Lipids –

  • Are insoluble in water!

  • Due to nonpolar C-H bonds

  • Known as fats and oils 


10. Describe the unique properties, building block molecules and biological importance of the three important groups of lipids: fats, phospholipids and steroids.

Fats – made with glycerol, a 3 carbon alcohol and a fatty acid (carboxylic with a hydrocarbon tail)

Used for:

  • Energy storage

  • Compact fuel reserves

  • Cushioning and insulating 


10 continued
10. Continued…. and biological importance of the three important groups of lipids: fats, phospholipids and steroids.

Phospholipids – made with a glycerol, 2 fatty acids, a phosphate group, and a small chemical group

Characteristics:

  • Tails are hydrophobic

  • Will cluster in water

  • Forms cell membrane bilayers 


10 continued1
10. Continued…. and biological importance of the three important groups of lipids: fats, phospholipids and steroids.

Steroids – are lipids that have 4 fused carbon rings with various functional groups attached

Example:

  • Cholesterol

    - precursor to sex hormones and bile acids

    - common in cell membranes

    -atheriosclerosis 


11 identify an ester linkage and describe how it is formed
11. Identify an ester linkage and describe how it is formed. and biological importance of the three important groups of lipids: fats, phospholipids and steroids.

Ester linkage –

  • Bond formed between a hydroxyl group (-OH) and a carboxyl group (-COOH)

  • Forms fat through condensation reactions that link glycerol to a fatty acid

    -OH + -COOH 


Saturated Fats and biological importance of the three important groups of lipids: fats, phospholipids and steroids.

No double bonds between carbons in tail

Has maximum number of hydrogens

Solid at room temperature – most animal fats

C-C-C-C

Unsaturated Fats

One or more double bonds in tail

Tail kinks at C=C so molecules do not pack closely enough to solidify

Liquid at room temperature – most plant fats

C=C-C=C 

12. Distinguish between saturated and unsaturated fat,and list some unique emergent properties that are a consequence of these structural differences.


13. Distinguish proteins from the other major classes of macromolecules and explain the biologically important functions of this group.

Proteins – a macromolecule that consists of one or more polypeptide chains folded and coiled into specific conformations

  • Made up of various 20 amino acids

  • Vary widely in structure and function

  • Abundant – about 50% of cellular dry weight (weight of cell minus water bulk) 


13 continued important functions
13. Continued…important functions macromolecules and explain the biologically important functions of this group.

  • Structural support

    2. Storage of amino acids

    3. Transport (hemoglobin)

    4. Signaling (chemical messengers)

    5. Cellular response to chemical stimuli (receptor proteins)

    6. Movement (contractile proteins)

    7. Defense against foreign substances & disease-causing organisms (antibodies)

    8. Catalysis of biochemical reactions (enzymes) 


14. List and recognize four major components of an amino acid, and explain how amino acids may be grouped according to the physical and chemical properties of the side chains.

Four components:

1. Hydrogen atom

2. Carboxyl group (-COOH)

3. Amino group (-NH2)

4. Variable ‘R’ group (specific to each amino acid)

- the properties of the side chain determine the uniqueness of each amino acid 


15 identify a peptide bond and explain how it is formed
15. acid, and explain how amino acids may be grouped according to the physical and chemical properties of the side chains.Identify a peptide bond and explain how it is formed.

Peptide bond = the covalent bond formed by a condensation reaction that links the carboxyl (-COOH) group of one amino acid to the amino (-NH2) group of another. 


16 explain what determines protein conformation and why it is important
16. Explain what determines protein acid, and explain how amino acids may be grouped according to the physical and chemical properties of the side chains.conformation and why it is important.

  • It is the 3D shape of a protein

  • Enables a protein to recognize & bind specifically to another molecule (ex: hormone receptor)

  • It is the consequence of the specific linear sequence of amino acids in the polypeptide

  • Produced when new chains coil & fold spontaneously (due to hydrophobic interactions)

  • It is stabilized by chemical bonds & weak interactions between neighboring regions of the folded protein 


17 define primary structure and describe how it may be deduced in the laboratory
17. acid, and explain how amino acids may be grouped according to the physical and chemical properties of the side chains.Define primary structure and describe how it may be deduced in the laboratory.

  • It is the unique sequence of amino acids in a protein

  • Determined by genes – slight changes can affect function (ex: sickle-cell)

    In a laboratory…

  • Determine amino acid composition by complete acid hydrolysis of peptide bonds – identify the aa’s and proportions

  • Determine the amino acid sequence by partial hydrolysis with enzymes and break specific peptide bonds – deductively reconstruct from fragments

  • Now automated sequencing 


18. Describe the two types of secondary protein structure, and explain the role of hydrogen bonds in maintaining the structure.

  • Coiling & folding of polypeptide backbone

  • H bonds between peptide linkages in the protein’s backbone help stabilize

  • Alpha helix

  • Helical coil stabilized by H bond every 4th peptide bond

  • Found in fibrous protein – collagen/elastin 


18 continued beta pleated sheet
18. Continued…Beta pleated sheet and explain the role of hydrogen bonds in maintaining the structure.

2. Beta pleated sheet

  • Sheet of antiparallel chains are folded into accordion pleats

  • Held together by H bonds

  • Dense core of globular proteins & some fibrous protein 


19 explain how weak interactions and disulfide bridges contribute to tertiary protein structure

Weak Interactions and explain the role of hydrogen bonds in maintaining the structure.

Hydrogen bonding between polar side chains

Ionic bonds between charged side chains

Hydrophobic interactions between nonpolar in interior

Covalent linkage

Disulfide bridges between 2 cysteine monomers brought together by folding

Reinforces conformation 

19. Explain how weak interactions and disulfide bridges contribute to tertiary protein structure.


20 using collagen and hemoglobin as examples describe quaternary protein structure

Collagen and explain the role of hydrogen bonds in maintaining the structure.

Fibrous protein with 3 helical polypeptides supercoiled into a triple helix

Hemoglobin

Four subunits grouped together (2 α chains and 2 β chains) 

20. Using collagen and hemoglobin as examples, describe quaternary protein structure.


21 define denaturation and explain how proteins may be denatured
21. and explain the role of hydrogen bonds in maintaining the structure.Define denaturation and explain how proteins may be denatured.

  • Is the process that alters a protein’s native conformation and biological activity

    Causes:

  • Transfer to an organic solvent-hydrophobic insides go out and vice versa

  • Chemical agents that disrupt hydrogen, ionic, and disulfide bonds

  • Excessive heat – thermal agitation disrupts the weak interactions 


22. Describe the characteristics that distinguish nucleic acids from the other major groups of macromolecules.

Nucleic acids –

  • Contain phosphorus

  • Store and transmit hereditary information

  • Are polymers of nucleotides

  • Determine protein structure, function, etc.

    Examples –

  • RNA (ribonucleic acid)

  • DNA (deoxyribonucleic acid) 


23 summarize the functions of nucleic acids
23. Summarize the functions of nucleic acids. acids from the other major groups of macromolecules.

  • To store and transmit hereditary information

    - directions for replication

    - information to run all cell activity

    - make up the genes for protein synthesis

    (the ‘brain’ for making anything) 


24. List the 3 major components of a nucleotide, and describe how these monomers are linked together to form a nucleic acid.

  • Pentose (5 carbon sugar)

    - ribose, deoxyribose

    2. Phosphate – attached to the 5th carbon of the sugar

    3. Nitrogenous base – pyrimidines & purines

  • Covalent bonds called phosphodiester linkages bond (between the phosphate of one sugar and the sugar of another) 


25 distinguish between a pyrimidine and a purine

Pyrimidine describe how these monomers are linked together to form a nucleic acid.

six-membered ring made up of carbon and nitrogen atoms

Ex: cytosine (C)

thymine (T) – DNA

uracil (U) – RNA

Purine

five-membered ring fused to a six-membered ring

Ex: Adenine (A)

Guanine (G)

25. Distinguish between a pyrimidine and a purine.


26 list the functions of nucleotides
26. List the functions of describe how these monomers are linked together to form a nucleic acid.nucleotides.

  • Monomers for nucleic acids

  • Transfer chemical energy from one molecule to another (ex: ATP )

  • Are electron acceptors in enzyme-controlled redox reactions of the cell (ex: NAD+) 


27 briefly describe the three dimensional structure of dna
27. Briefly describe the three-dimensional structure of DNA. describe how these monomers are linked together to form a nucleic acid.

  • Consists of 2 nucleotidechains wound in a double helix

  • Sugar-phosphate backbones on the outside

  • 2 strands held together by hydrogen bonds between the paired nitrogenous bases

  • Van der waals attraction between stacked bases

  • 2 DNA strands are complementary and serve as templates for new strands

  • Long – 1000’s or millions of base pairs 


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