BMS02-1005/49 Protein Structure Flashcards

1
Q

What makes up cementum? (2)

A

Collagen

Glycoproteins

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2
Q

What makes up dentin? (3)

A

Collagen
Glycoproteins
Proteoglycans

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3
Q

What makes up enamel? (2)

A

Amelogenins

Enamelins

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4
Q

Glycine

A

H

Non polar

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5
Q

Alanine structure

A

CH3

Non polar

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6
Q

Valine

A

Non polar

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7
Q

Leucine

A

Non polar

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8
Q

Serine

A

CH2 OH
Uncharged
Polar

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9
Q

Phenylalanine structure

A

CH2 benzene

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10
Q

Tyrosine

A

Uncharged

Polar

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11
Q

Cysteine

A

CH2 SH

Non polar

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12
Q

Asparagine structure

A

Uncharged

Polar

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13
Q

Glutamine structure

A

Uncharged

Polar

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14
Q

Aspartic acid

A

Negative

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15
Q

Glutamic acid

A

Negative

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16
Q

Histidine

A

Positive

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17
Q

Lysine

A

Positive

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18
Q

Arginine

A

Positive

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19
Q

Name the 3 bases

A

Lysine
Histidine
Arginine

20
Q

Name the 3 acids

A

Glutamine
Aspartic acid
Glutamic acid

21
Q

Phenylalanine

22
Q

Proline

23
Q

What is the N and C terminal?

A

The free NH3+

The free COO-

24
Q

Describe the peptide bone resonance structure

A

CN bond is shorter and is a double with the N +

CO is a single and the O is -

25
Which bond in AA is especially rigid?
CN
26
Describe the primary structure
Sequence of AA, main force is hydrophobic
27
Describe the secondary structure
HB into alpha helix or beta pleated
28
Describe the tertiary structure
The chain folds upon itself, philic, phobic, ionic, disulphide etc due to side chain interactions
29
Describe the special properties of cysteine (4)
Is a very reactive group Strong reducing agent Forms strong covalent bonds Easily oxidised to form a dimer
30
Describe the hydrogen bond
Strongest idid | OH, NH, F
31
Where does the hydrogen bond form
Between the amino group and the double bonded oxygen at every 4th peptide
32
Where do side chains lie in the beta pleat?
Above and below the plane sheet
33
Name the 2 types of beta pleat
Antiparallel (S shaped) and parallel (dome over the top)
34
If a protein has lots of beta pleats what does this indicate?
No elasticity and high strength
35
What is the supersecondary structure?
Combinations of the secondary structure
36
Name some common domains
B barrel A B barrel B hairpin Rossman fold (3 B)
37
Domain 1
A B barrel
38
Domain 2
B barrel
39
Domain 3
A B sheet
40
Name the 3 post translational modifications
Glycosylation Addition of sugar Can be O linked or N linked Phosphorylation Turns on protein kinase or enzymes Methylation NH2 groups in lysine and arginine
41
What are the 2 modified proteins in collagen?
Hydroyproline and hydroxylsyine
42
What are the 3 AA in collagen?
Glycine | Mainly proline and hydroxyl-proline
43
Examples of type 1 collagen
Skin, bone, tendon, dentine
44
Examples of type 2 collagen
Cartilage
45
Examples of type 3 collagen
Blood vessels Lungs Pulp
46
What happens in scurvy?
Unstable collagen so you bruise easy, old wounds reopen, gums bleed, bad healing and GI bleeds