Proteins, Polysaccharides and Lipids Flashcards

1
Q

What is the primary structure of a protein?

A

Amino Acid chain linked together by peptide bonds

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2
Q

What are the 3 types of secondary protein structures?

A

-Alpha Helix
-Beta Sheet
-Triple Helix

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3
Q

Describe the alpha helix structure of a secondary protein
Structure?
Where are they found?
What are they stabilised by?
The Co of each amino acid is bonded to what?
How many residues per turn

A

-Rod like, right handed
- Found in strong, extensible proteins
-Stabilised by Hydrogen Bonds
-CO of each amino acid is H bonded to NH of amino acid four residues ahead in sequence
-3.6 Residues per helix/ turn

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4
Q

Give examples of alpha helix secondary proteins

A

Haemoglobin, Myoglobin, Keratins, Fibrins, Myosin

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5
Q

Describe the Beta Pleated sheet structure of secondary proteins and where are they found

A

-Zigzag chains
-Place several chains side by side, CO and NH groups align, H-bonding occurs → sheet-like structure
-Parallel: chains run in same direction
-Anti-parallel: chains run in opposite
directions
-Found in proteins where flexibility needed eg. silk fibroin (anti-parallel arrangement

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6
Q

Describe the triple helix structures of secondary proteins

A

-Collagen only
-Major component of connective tissue (skin, bone, tendon)
-Very strong, water-insoluble fibres
-Three chains wound round each other (rope) → tropocollagen
-~ 1000 amino acids per chain
-No H bonds in each chain

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7
Q

What repeating structure does each chain have in triple helix secondary proteins?

A

X- Pro- Gly

OR

X- Hyp- Gly

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7
Q

What repeating structure does each chain have in triple helix secondary proteins?

A

X- Pro- Gly

OR

X- Hyp- Gly

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8
Q

By what bonds are the three strands in triple helix secondary proteins held together by?

A

Hydrogen bonds by HYP and Hydroxylysine residues

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9
Q

By what bonds are the three strands in triple helix secondary proteins held together by?

A

Hydrogen bonds by HYP and Hydroxylysine residues

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10
Q

What sits inside the helix and what projects out of the helix of triple helix secondary proteins?

A

-Small Gly residues sit inside helix
-BulkyR groups either side of Gly project outwards

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11
Q

How is the triple helix intra and intermolecularly cross linked?

A

By covalent bonds between Lys and His

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12
Q

Describe fibrous proteins.

A

Insoluble, Metabolically unreactive

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13
Q

What are fibrous proteins mainly? Give examples.

A

Structural Proteins;

-collagen
-keratin (skin, hair, nails, fur, wool)
-fibrin (bloot clots)
-elastin (elastic fibres of connective tissue eg. arterial walls)
-myosin (muscle)

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14
Q

Describe globular proteins

A

Spherical

Backbone folds on itself

Water-soluble, compact structures

Usually have 3º and 4º structures eg. myoglobin and actin (3º), haemoglobin (4º)

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15
Q

What does the interior of myoglobin contain?

A

Entirely non-polar residues except for two polar His residues (attachment and function of Haem group)

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16
Q

What is myoglobin used for?

A

Oxygen storage in muscle

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17
Q

What type of protein is myoglobin and what structures is it associated with?

A

Globular, associated with 3º structures

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18
Q

How Many chains does myoglobin have?

A

Single chain (153 aa)

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19
Q

How Many chains does myoglobin have?

A

Single chain (153 aa)

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20
Q

How many helical regions in myoglobin

A

8 (75% of all aa)

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21
Q

Is there beta pleated sheet regions in myoglobin?

A

No

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22
Q

How are the helical segments of myoglobin joined?

A

Regions of random coiling where chain makes major directional change

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23
Q

What group does myoglobin contain and how is it bound/ where is it?

A

in hydrophobic pocket, held in position by hydrophobic interactions between haem porphyrin ring and non-polar side chains of aa in surrounding helical segments

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24
What happens to myoglobin if harm group is absent
apoprotein, not as tightly folded
25
Haemoglobin function?
oxygen Transport
26
What structures is haemoglobin associated with?
Quaternary Structures
27
How many polypeptide chains are in haemoglobin and what do they look like?
Two pairs of polypeptide chains ( 2 Alpha 2 beta) folded into a similar shape to myoglobin
28
Shape of haemoglobin molecule?
Spheroidal Molecule
29
How many ham groups in haemoglobin and where do they lie in the molecule?
Four Haem groups, lie on surface of molecule in individual pockets, far apart
30
How many amino acids on alpha chains of haemoglobin? How many amino acids on beta chains of haemoglobin?
- Alpha- 141 - Beta- 146
31
What is each alpha unit in contact with in haemoglobin?
Both Beta Chains
32
Describe the structure of each chain and what forms when they are fitted together
α1β1 and α2β2 half-molecules irregular in shape → central open channel when fitted together
33
What are peripheral membrane proteins located?
Lie on membrane surface
34
Where are integral membrane proteins located?
Within Lipid Bilayer
35
What do channel proteins do?
Form a channel in membranes and facilitate movement of small molecules across the membrane (simple diffusion)
36
What do carrier proteins do?
Bind to transported molecules (facilitated diffusion)
37
Give an example of messenger proteins
Hormones
38
What is the function of hormones?
Allows cells to communicate with each other
39
Give 3 modes of action of hormones
1. Influence rate of synthesis of enzymes and other proteins 2. Affect rate of enzymatic catalysis 3. Alter permeability of cell membranes
40
What does each hormone have?
Its own corresponding receptor
41
Describe the action of hormones binding to receptors?
Hormone binds receptor → message relayed to inside of cell → cascade of events → cellular action
42
Give examples of hormones
Insulin Glucagon Human Growth Hormone
43
What is the function of insulin?
Sugar uptake by cells from bloodstream
44
What is the function of Glucagon
Sugar release by cells into bloodstream
45
Hormones can be what?
-Protein/Polypetide -Amino Acid Derivatives -Steroid
46
Describe Enzymes; What are they? Protein Type? Function? Specificity?
-Biological Catalysts -Globular Proteins -Increase reaction rates up to 10^20 -Highly Specific (reaction, substrate)
47
Give examples of muscular contraction messenger proteins ? and their type
- Myosin- fibrous - Actin- globular
48
Give examples of messenger proteins used in immune protection
-Cytokines -Antibodies
49
What are the monomers of polysaccharides?
Monosaccharides
50
What are two functions of polysaccharides?
-Storage -Structure
51
Give examples of two storage polysaccharides
Glycogen, Strarch
52
Give examples of three Structure Polysaccharides
Cellulose, Chondroitin, Sulphate, Peptidoglycan
53
What are two types of monosaccharides?
-Aldoses -Ketoses
54
What are aldoses?
Monosaccharides that contain the aldehyde (CHO) group
55
What are ketoses?
Monosaccharides that contain the ketone (CO) group
56
What are monosaccharides?
The building blocks of complex carbohydrates
57
give a example of a monosaccharide
GLUCOSE
58
Formation of Disaccharides?
Dehydration reactions of monosaccharide units form complex carbohydrates
59
Breakdown of Disaccharides?
Hydrolysis reactions of monosaccharide units catabolise complex carbohydrates
60
What are polysaccharides
Isomers of monosaccharides give rise to a huge variety of polysaccharides
61
what are the monomers of lipids?
Fatty acids
62
What are the main types of lipids?
Triglycerides Diglycerides Sterols
63
Give 2 functions of lipids
-Storage -Membrane Structure
64
What are glycerides based on
Glycerol
65
What are -Glycerides -Diglycerides -Triglycerides made up of
GLYCEROL FATTY ACID 1 1 1 2 1 3
66
Glyceride structure diagram;
67
Give an example of a diglyceride and its function
phosphoatidylcholine- a major phospholipid of membranes
68
What are triglycerides role?
Storage compounds
69
What are diacylglycerides used for?
Major components of biological membranes
70
The degree of saturation of fatty acids (acyl lipids) affects what?
-Van der Waals forces -Changes lipid physical properties
71
Sterols function?
some have essential biological activity Others are important constituents of biological membranes