Carbohydrates, Lipids and Proteins (SR) Flashcards

(39 cards)

1
Q

What are Monomers?

A

Individual molecules that make up a polymer

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2
Q

What are Polymers?

A

Long chains
Composed of multiple Monomers
Bonded together in Repeating Pattern

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3
Q

When does a Condensation Reaction Occur?

A

Occurs when two molecules combine to form a more complex molecule with removal of water

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4
Q

When does a Hydrolysis Reaction Occur?

A

When larger molecules are broken down into smaller ones with the addition of water

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5
Q

What are Monosaccharides?

A

Simplest Carbohydrates

Consisting of only one Sugar molecule (Glucose, Fructose & Galactose)

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6
Q

What is Glucose?

A

A Hexose sugar with 2 Isomers:
α-Glucose
β-Glucose

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7
Q

What are Disaccharides?

A

Sugars that are composed of two Monosaccharides
Joined together in a condensation reaction
Forming a Glycosidic Bond

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8
Q

What is an example of a polysaccharide and is the main energy store in plants?

A

Amylopectin (Starch)

Composed of α-Glucose

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9
Q

What is an example of a polysaccharide used for energy store in animals?

A

Glycogen

Composed of α-Glucose

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10
Q

What is an example of a polysaccharide that is used as a structural component?

A

Cellulose

Composed of long unbranched chains of β-Glucose

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11
Q

What are the two types of Fatty Acids?

A

1) Saturated

2) Unsaturated

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12
Q

What is the difference between a Saturated Fatty Acid and an Unsaturated Fatty Acid?

A

Saturated has no C=C double bonds, as many hydrogens as possible

Unsaturated has at least 1 C=C double bond, therefore contains less Hydrogen, C=C bond causes a kink so can’t be closely packed together, which means it is liquid at room temp

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13
Q

What is a triglyceride molecule?

A

Formed by joining one molecule of Glycerol to 3 Fatty Acids
Done by 3 Condensation Reactions
Forming Ester Bonds

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14
Q

How do Triglycerides have key roles in Respiration and Energy Storage?

A

Due to its Insolubility and High Carbon : Hydrogen Ratio

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15
Q

What is the difference between a Phospholipid and a Triglyceride?

A

Triglyceride has 3 Fatty Acid Chains

Phospholipid has 2 Fatty Acid Chains and a Phosphate molecule

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16
Q

How do the properties of Phospholipids make them great for cell-surface membranes?

A
Hydrophobic Tails (fatty acids & glycerol) - Non-polar and insoluble in water (inner layer)
Hydrophilic Head (Phosphate) - Polar and soluble in water
Overall forms Phospholipid Bilayer (outer layer)
17
Q

What are Amino Acids?

A

Monomer Units used to make Proteins

18
Q

How many naturally occurring Amino Acids are there?

A

20

Only difference is the R Group

19
Q

What are Dipeptides and how are they formed?

A

Two amino Acids
Joined together by Condensation Reaction
Forming Peptide Bond

20
Q

What is a Polypeptide?

A

Polymer made of many Amino Acids

Joined together by Peptide bonds

21
Q

What are the 4 Structural Layers (Structures) of Proteins?

A

1) Primary (1º)
2) Secondary (2º)
3) Tertiary
4) Quaternary

22
Q

What is the Primary Structure (1º)?

A

Specific Sequence of Amino Acids in a Polypeptide Chain

Peptide Bonds hold them together

23
Q

What is the Secondary Structure (2º)?

A

Curling or Folding of Polypeptide Chain
Into α-helices and β-pleated sheets due to formation of H-Bonds

Hydrogen Bonds (H-Bonds) hold it together

24
Q

What is the Tertiary Structure?

A

Overall Specific 3D Shape of a Protein, determined by interactions b/w R groups and properties of R groups

Hydrogen Bonds, Ionic Bonds and Disulphide Bridges hold them together

25
What is the Quaternary Structure?
Specific 3D shape of a protein determined by the multiple polypeptide chains and/or prosthetic groups bonded together Hydrogen Bonds, Ionic Bonds and Disulphide Bridges hold them together
26
How do you test for Reducing Sugars?
Benedict's Reagent Reducing Sugar Reduces Cu (II) to Cu (I) Changes from Blue to Brick Red/Orange ppt formed
27
What is the test for Starch?
Iodine in Potassium Iodide solution | Sample changes from Brown-Orange to dark Blue/Black if Starch present
28
How do you test for Non-Reducing Sugars?
Break down into Reducing sugars by heating w/diluted HCl or hydrolyse using Enzymes Neutralise solution using Sodium Hydrogencarbonate Continue with Benedict's Reagent Brick Red/Orange ppt formed if reducing sugar present
29
How do you test for Proteins?
Biuret Test Add Sodium/Potassium Hydroxide to solution containing crushed up/dissolved proteins/food to make solution alkaline Shake Add Copper (II) Sulphate Solution Solution should go from Blue to Purple if Proteins present
30
How do you test for Lipids?
Emulsion Test Add Ethanol to test solution and shake for approx 1 min so it dissolves Add Water to the solution Any lipid will show as a milky white emulsion, the more lipid there is, the more noticeable the emulsion is Test can be Improved by adding Sudan III to stain Lipids Red
31
What are Enzymes?
Biological Catalysts That speed up Rate of Reaction Remains Unchanged and re-usable @ end of reaction
32
How do enzymes work?
They lower the Activation Energy
33
What was the old theory for Enzyme Action?
Lock and Key | Each substrate is a 'key' and only fits to specific 'lock' (enzyme)
34
What is the alternative theory for Enzyme Action?
Induced Fit: Substrate Induces change in enzyme so that it fits Enzyme when it contacts, moulds around Substrate Conformational change so enzyme moulds to fit substrate
35
What is the Specificity of Enzymes down to?
Due to Tertiary Structure of Active Site | Allowing Complementary binding to Substrates
36
What types of Reactions do Enzymes Catalyse?
Both Intra- and Extracellular reactions | That determine structures and functions from cellular to whole organism levels
37
What factors affect Enzyme Activity?
1) pH 2) Temperature 3) Enzyme Concentration 4) Substrate Concentration 5) Competitive & Non-Competitive Inhibitor Conc.
38
What is Competitive Inhibition?
Inhibition of Enzyme that is Reversible Can be overcome by increasing amount of Substrate Irreversible bonding called an Inactivator Level of Inhibition depends on conc. of Substrates
39
What is Non-Competitive Inhibition?
``` When Inhibitor Binds to Allosteric Site Alters Specific shape of Enzymes Tertiary Site (Active Site) Disrupts shape of active sites Substrate can no-longer bind to Enzyme IRREVERSIBLE ```