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Biomed > Biochem > Flashcards

Biochem Flashcards

1
Q

Types of proteins

A

Fibrous and globular

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2
Q

Properties of fibrous proteins

A

Insoluble in water
Important structural proteins

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3
Q

Types of fibrous proteins (7)

A

Collagens
Keratin
Fibrin
Elastins
Myosin
Actin
Fibroin

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4
Q

Properties of collagen (2)

A

25-35% total protein in mammals
Major component of connective tissues

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5
Q

Properties of keratin (2)

A

Composed of a helix structure
Basic unit of structure is the protofibril

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6
Q

Properties of globular proteins (2)

A

Roughly spherical in shape
More soluble than fibrous proteins

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7
Q

Types of globular proteins (6)

A

Enzymes
Peptide hormone
Haemoglobin
Myoglobin
Albumin
Antibodies

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8
Q

What is a conjugated protein?

A

Contains a protein component associated with a non-protein component

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9
Q

Types of conjugated proteins (4)

A

Lipoproteins
Glycoproteins
Nucleoproteins
Metalloproteins

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10
Q

Properties of aliphatic amino acids (3)

A

C atoms in side chain are arranged in chains
Non-polar covalent bonds
Weak hydrophobic

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11
Q

Properties of hydroxy amino acids (3)

A

OH groups in side chains
Make polar bonds
Hydrophilic

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12
Q

Properties of sulphur-containing amino acids (3)

A

Aliphatic side chains
Thiol or thioether groups
Hydrophobic

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13
Q

Properties of aromatic amino acids (2)

A

Side chains contain benzene skeleton
Hydrophobic

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14
Q

Properties of heterocyclic amino acids (3)

A

Histine
Ring structure is not composed of one atom
Hydrophilic

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15
Q

Properties of basic amino acids (2)

A

Positively charged at a neutral pH
Hydrophilic

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16
Q

Properties of acidic amino acids (4)

A

Negatively charged at a neutral pH
Secondary carboxylate acid group
Amide group of CONH2
Hydrophilic

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17
Q

Properties of imino acids (2)

A

Aliphatic side chain
Hydrophobic

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18
Q

What are amino acids joined by?

A

Peptide bonds

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19
Q

What are all 20 amino acids used for?

A

To synthesise proteins

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20
Q

What is primary structure?

A

The sequence of amino acids of a polypeptide

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21
Q

What are the other levels of protein structure? (4)

A

Secondary structure
Tertiary structure
Quarternary structure

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22
Q

Process of amino acids polymerised into peptides and polypeptides

A

Catalysed by peptidyl transferase enzymes
Requires a template
Is a dehydration reaction
Via peptide bonds

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23
Q

When is a peptide bond formed?

A

When the a-carbonyl group of the first amino acid convalently links the a-amino group of the second amino acid

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24
Q

What is an oligopeptide?

A

A chain of amino acids residues linked by peptide bonds

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25
Q

What is the primary structure of bovine ribonuclease?

A

124 amino acids
4 disulphide bonds

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26
Q

Properties of a secondary structure

A

Certain arrangements that stabilises the protein
3D structure
Included alpha helix and beta pleated sheet

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27
Q

Structure of alpha helix

A

Cylinder shape
Held together by hydrogen bonds
Turns clockwise

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28
Q

What is an imino acid (proline)?

A

Helix breaker
Has a side chain which neighbouring residue can join

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29
Q

Properties of a beta pleated sheets

A

Extended polypeptide chains
Stabilised by hydrogen bonding with amino acids in other strands
Can link different regions with a single polypeptide
May be parallel or anti-parallel

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30
Q

Properties of tertiary structure

A

3D structure of an entire globular protein in its biologically active shape
Normally stabilised by non-covalent interactions between side chains
Compactly folded regions called domains

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31
Q

Types of dietary lipids (3)

A

Triglycerides
Chloesterol
Phospholipids

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32
Q

Types of triglycerides (4)

A

SFAs
Trans FAs
MUFAs
PUFAs

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33
Q

What does cholesterol make? (4)

A

Bile acids
Vitamin D
Steroid hormones
Cell membranes

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34
Q

What are dietary proteins for?

A

To build and repair tissue
Growth and development
Building blocks

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35
Q

What does excessive protein do to the body?

A

Kidney damage
Increased cancer risk
Possible dehydration
Constipation

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36
Q

What can excessive lipid do to the body?

A

Raised chloesterol
Increased risk of heart disease

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37
Q

What is an acid?

A

A molecule that acts as a proton donor

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38
Q

What is a base?

A

A molecule that acts as a proton acceptor

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39
Q

Alpha amino groups

A

NH2 or NH3+

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40
Q

Alpha carboxyl group

A

COO- or COOH

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41
Q

Side chains (7)

A

Asp, glu, lys, arg, his, cys, tyr

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42
Q

What are properties of amino acids that influence 3D structure (3)?

A

Aromatic stacking
Hydrogen bonding
Binding of metallic cations

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43
Q

What structure will denature an enzyme is disrupted?

A

Tertiary

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44
Q

What is a mutation?

A

A change in the DNA sequence of the gene encoding a protein.

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45
Q

How are peptide bonds broken?

A

Hydrolysis

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46
Q

What are the different types of proteins? (5)

A

Lipoproteins
Glycoproteins
Phosphoproteins
Hemoproteins
Metalloproteins
Oligomeric proteins

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47
Q

What are lipoproteins?

A

Proteins with fats attached to them.

48
Q

What are glycoproteins?

A

Proteins with sugar attached to them.

49
Q

What are phosphoproteins?

A

Proteins with phosphate groups attached to them.

50
Q

What are hemoproteins?

A

Proteins with co-factors attached to them.

51
Q

What are metalloproteins?

A

Proteins with metal ions attached to them.

52
Q

What are oligomeric proteins?

A

Proteins consisting of more than one subunit.

53
Q

What are the properties of lipids?

A

They are all insoluble in water and soluble in organic solvents.

54
Q

What are the functions of lipids? (3)

A

They are structural components of biological membranes
They are energy reserves (mainly in the form of triacylglycerols)
Serves as vitamins and hormones

55
Q

Types of lipids (7)

A

Fatty acids
Triacylglycerols
Phospholipids
Glycolipids
Prostaglandins
Terpenes
Steroids

56
Q

What is the difference between saturated and unsaturated fatty acids?

A

Unsaturated have a cis double bonds and saturated have a trans double bond.

57
Q

How does chain length affect fatty acids?

A

The longer the fatty acid, the higher the melting point.

58
Q

How does saturation affect fatty acids?

A

The more saturated, the higher the melting point.

59
Q

Why are triacylglycerols important?

A

They serve as insulation and cushioning from mechanical injury and stored as adipose tissue.

60
Q

What are triacylglycerols?

A

3 fatty acids and 1 molecule of glycerol.

61
Q

Properties of triacylglycerols?

A

Oxidised by atmospheric oxygen
Hydrolysed by atmospheric water

62
Q

How is soap made?

A

Hydrolysis of triacylglycerols.

63
Q

How do phospholipids help the body?

A

Important constituents of all biological membranes.

64
Q

What are phospholipids constructed from?

A

Fatty acids
Platform to which fatty acids are attached
Phosphate group
Alcohol attached to phosphate group

65
Q

Why are phospholipids amphipathic?

A

They have 2 long hydrophobic tails and a hydrophilic head.

66
Q

How do glycolipids help the body?

A

They are important components of cell membrane.

67
Q

Glycolipid structure

A

Contain one or more sugars

68
Q

How do protstaglandins help the body?

A

They act as local hormones.

69
Q

Roles of prostaglandins (6)

A

Stimulate inflammation
Stimulate smooth muscle contraction
Regulate blood flow to particular organs
Affect platelet aggregation
Modulate synaptic transmission
Induce sleep

70
Q

Why are terpenes important?

A

They are videos occurring in nature and some are pungent.

71
Q

Structure of terpenes

A

Same 5 car in building block.

72
Q

What do steroids have roles in? (5)

A

Solubilisation of dietary lipids
Preparation and maintenance of pregnancy
Stress response
Sexual characteristics
Regulation of membrane fluidity

73
Q

Structure of steroids.

A

6 isoprene units
Tetracycline ring structure

74
Q

What do living things require a continual I put of free energy for?

A

Synthesis and maintenance
Performance of mechanical work
Active transport of substances into and out cells

75
Q

Where is the energy derived from?

A

Chemotrophs (chemicals)
Phototrophs (light)

76
Q

Processes that release energy are…

A

Favoured

77
Q

Processes that require energy is…

A

Not favoured

78
Q

Burning of coal equation.

A

C + O2 -> CO2 + heat

79
Q

Production of energy equation.

A

C6H12O6 + 6O2 -> 6CO2 + 6H2O + free ENERGY

80
Q

What is substrate level phosphorylation?

A

Direct transfer of phosphate gp from metabolites to ADP producing ATP.

81
Q

What is oxidative phosphorylation?

A

ATP formed indirectly from oxidation of carbon atoms in fuel molecules.

82
Q

What does the electron transport chain do?

A

Couples energy release from oxidation to energy requiring H+ pumping across inner membrane into inter membrane space.

83
Q

What is the immediate source of energy?

A

Glucose.

84
Q

What else can be used for energy?

A

Glycogen
Fats
Proteins

85
Q

What is the biggest energy storage?

A

Fats

86
Q

What is the major site of fat accumulation?

A

Adipose tissue.

87
Q

Beta oxidation reaction
Oranges Have an Orangey Taste

A

1st oxidation
Hydration
2nd oxidation
Thiolysis

88
Q

What does coenzyme A do?

A

Pick up, carry and drop metabolites and funnel them into whatever pathways are needed.
Also bind to FAs and break them down aerobically for energy

89
Q

1st oxidation

A

Saturated acyl CoA is oxidised to an unsaturated trans-acyl CoA (enoyl CoA) containing a double bonds at its beta-carbon atom.

90
Q

Hydration

A

Enoyl CoA double bond is hydrated so saturated hydroxyacyl CoA forms
Catalysed by enoyl CoA hydratase

91
Q

2nd oxidation

A

The beta carbon of hydroxylacyl CoAs hydroxyl group is oxydysed by a keto group forming unsaturated 3-Ketoacyl CoA

92
Q

Thiolysis

A

Thiol group of a 2nd CoA molecule attacks the c bond of 3-ketoacyl CoA causing cleavage of this bond and liberations a 2-carbon unit binding to CoA and forms acetyl CoA
Catalysed by beta-keto thiolase

93
Q

Ketogenesis

A

A different way fat can be broken down in the liver when the balance between carbohydrates and fat metabolism shifts towards fat breakdown.

94
Q

Formation of ketone bodies.

A

Ketone bodies diffuse out of the mitochondria and out of the hepatocytes
Enter the circulation and are taken up as a fuel source by non-hepatic tissues.

95
Q

Protein/amino acid catabolism

A

Proteins are degraded to amino acids
Amino acids are degraded to amino croups and carbon skeleton
Carbon skeletons can be used catabollically as fuel
Excretion of excess nitrogen

96
Q

Functions of carbohydrates (3)

A

Storage of energy
Structural
Specialised roles when modified or complexed with other macromolecules

97
Q

Types of unmodified carbohydrates (4)

A

Monosaccharides
Disaccharides
Oligosaccharides
Polysaccharides

98
Q

What are monosaccharides?

A

Simple sugars
Colourless or white crystalline solids
Water soluble
Open chain and ring structures

99
Q

What are disaccharides?

A

2 linked monosaccharides

100
Q

What are oligosaccharides?

A

Short chains (less than 20 residues)

101
Q

What are polysaccharides?

A

100s or 1000s of units

102
Q

Properties of aldoses.

A

Carbonyl at the end of chain = aldehyde
Reducing sugars
Asymmetric chiral centres at C2, C3, C4 and C5

103
Q

Properties of ketoses.

A

Carbonyl group at C2 position = ketone
Non-reducing sugar
Asymmetric chiral centres at C3, C4 and C5

104
Q

What are aldehydes acting as when oxidised?

A

Reducing agents.

105
Q

Can ketones be oxidised?

A

No, only reduced to form alcohols.

106
Q

Where do we get carbohydrates?

A

Hydrolysis of starch

107
Q

Where is a glycosidic bond present?

A

Between C1 of one sugar and an -OH group at any position on the other sugar.

108
Q

What reaction is glycosidic bond formation?

A

A condensation reaction.

109
Q

Glucose disaccharides (3).

A

Trehalose
Maltose
Cellobiose

110
Q

Functions of polysaccharides.

A

Storage of energy
Structural

111
Q

2 important polysaccharides.

A

Glycogen and starch.

112
Q

Where is glycogen stored?

A

Skeletal muscle
Liver

113
Q

What is required for glycogen synthesis?

A

Glycogen synthase
Primer
Branching enzyme

114
Q

What is maltodextrin?

A

A polysaccharides which is a preservative.

115
Q

What are beta glucans good for?

A

Lowering cholesterol
Slows passage of food (making u full for longer)
Decreases inflammation

Biomed (3 decks)

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