Proteins, Polysaccharides And Lipids Flashcards

1
Q

A-helix examples

A

Haemoglobin, Myosin

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

A helix bonding

A

CO hydrogen bonded to NH 4 residues ahead.

3.6 residues / helix turn

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

A helix structure

A

Rod. Strong extensible proteins. Stabilised by H bonds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

Beta Pleated Sheet example

A

Proteins where flexibility eg silk fibroin (anti-parallel)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

Beta pleated sheet structure

A

Zigzag chains. Parallel, Anti-parallel

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

Beta pleated sheets bonding

A

Chains align, CO and NH align, H bonding occurs = sheet structure

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

Triple Helix example

A

Collagen only. Connective tissue (skin, bone, tendon)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

Triple helix structure

A

Strong soluble fibres. Three chains = tropocollagen

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Triple helix amino acid number

A

1000 per chain. No H bonds in chain

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

Triple Helix chemical structure

A

X-Pro-Gly or X-Hyp-Gly. H bonds between Hyp and Hydroxylysine residues

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

Triple Helix 2

A

Small Gly residues. Bulky R groups point outwards. Intra/inter covalent bonds between Lys and His

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

Fibrous proteins

A

Insoluble, metabolically unreactive.
Collagen
Keratin
Fibrin (blood clots)
Elastin (eg arterial walls)
Myosin (muscle)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

Physical structure of collagen triple helix

A

Glycine, hydroxyproline, proline

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

Globular proteins

A

Spherical. Backbone folds on itself. Soluble

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

Globular proteins structure

A

Usually have 3• and 4• structures eg myoglobin and actin (3•) and haemoglobin (4•)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Sterols examples

A

Cortisol, Cholesterol, Estrogen (estradiol) , testosterone

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

Stearic acid (saturated fat and fatty acid)

A

the molecules are tightly packed

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

Unsaturated fat and fatty acids (oleic acid)

A

The molecules cannot pack together closely due to kinks

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

Myoglobin

A

Oxygen storage in muscle. Globular, 3* structures. 8 helical regions (75 percent of all aa), single chain (153 aa), random coiling

20
Q

Absence of haem group in myoglobin

A

Forms apoprotein
not tightly folded

21
Q

Myoglobin interior

A

only two polar His residues Important for haem

22
Q

Prosthetic haem group

A

hydrophobic bonds between haem porphyrin ring and non polar side chains

23
Q

Haemoglobin

A

Oxygen transport. 4* structures. 2 pairs of polypeptide chains (2a and 2b) Similar to myoglobin. Spheroidal. 4 haem groups

24
Q

Interactions Haemoglobin

A

Each a subunit in contact with both b chains. Few interactions between two a or two b chains.

25
Q

Irregular shape

A

a1b1 and a2b2 half molecules irregular in shape as central open channel when fitted together

26
Q

Mode of action of messenger proteins

A

Influence rate of synthesis of enzymes and other proteins

Affect rate of enzymatic catalysis

Alter permeability of cell membranes

27
Q

Hormone

A

Bonds membrane bound receptor, message related to inside cell, cascade of events, cellular action

28
Q

Hormones can be

A

Proteins polypeptide amino acid derivatives or steroids

29
Q

Enzymes

A

Globular proteins that increase reaction rates by up to 10^20

30
Q

Muscle contraction

A

Myosin (fibrous)

Actin (gobular)

31
Q

Immune protection

A

Antibodies, cytokines

32
Q

Monosaccharides

A

The building blocks of more complex carbohydrates

33
Q

Aldoses vs ketoses

A

Aldoses contain aldehyde group and ketoses contain ketone group

34
Q

Starch vs cellulose

A

Starch has 1-4 linkages of a glucose whilst cellulose has 1-4 linkages of b glucose

35
Q

Disacchardides

A

Dehydration/hydrolysis reactions of monosaccharide units form /catabolise complex carbohydrates

36
Q

Glucose plus glucose

A

Maltose

37
Q

Sucrose plus maltose

A

Lactose

38
Q

Difference between alpha and beta configuration

A

OH in alpha below 1 and above 1 in beta

39
Q

Starch vs cellulose up or down

A

Starch down but cellulose up

40
Q

Amylose

A

Unbranched (5-600 glucose units) a-1,4-linked

41
Q

Amylopectin

A

Branched glucose units. 30 a-1,4-linked units until branch point (a-1,6 link)
Food reserve

42
Q

Glycogen

A

Same structure as starch but more highly branched
Food reserve

43
Q

Cellulose

A

Unbranched b-1,4-linked glucose units
Cannot be digested by animal enzymes (some ruminants possess b-glycosidases which digest cellulose)
Structural role

44
Q

Complex carbohydrates

A

Plant cells, cellulose microfibrils in plant cell wall (0.5 micro metres), microfibril, about 80 cellulose molecules form a microfibril the main architectural unit of a plant cell wall. Cellulose molecules, a cellulose molecule is an Unbranched b glucose polymer. Parallel cellulose molecules held by hydrogen bonds between hydroxyl groups attached to carbons 3 and 6

45
Q

Glycerides (based on glycerol)

A

For example phosphatidylcholine (a diacylglyceride) is a major phospholipid of membranes. Triacylglycerides are storage compounds