Proteins, Polysaccharides And Lipids Flashcards

1
Q

A-helix examples

A

Haemoglobin, Myoglobin, Keratins, Fibrins, Myosin

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2
Q

A helix bonding

A

CO of each amino acid hydrogen bonded to NH of amino acids 4 residues ahead.

3.6 residues / helix turn

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3
Q

A helix structure

A

Rod like right handed. Found in strong extensible proteins. Stabilised by hydrogen bonds

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4
Q

Beta Pleated Sheet example

A

Found in proteins where flexibility needed eg silk fibroin (anti-parallel)

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5
Q

Beta pleated sheet structure

A

Zigzag chains. Parallel = chains run in same direction
Antiparallel = chains run in opposite directions

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6
Q

Beta pleated sheets bonding

A

Several chains side by side, CO and NH groups align, hydrogen bonding occurs creating a sheet like structure

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7
Q

Triple Helix example

A

Collagen only. Major component of connective tissue (skin, bone, tendon)

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8
Q

Triple helix structure

A

Very strong water soluble fibres. Three chains wound round each other (rope) creating a tropocollagen

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9
Q

Triple helix amino acid number

A

1000 per chain. No H bonds in chain

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10
Q

Triple Helix chemical structure

A

Each chain had repeating structure of either X-Pro-Gly or X-Hyp-Gly. Three strands held together by H bonds between Hyp and Hydroxylysine residues

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11
Q

Triple Helix 2

A

Small Gly residues inside helix. Bulky R groups on either side point outwards. Intra and inter molecularly cross linked by covalent bonds between Lys and His

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12
Q

Fibrous proteins

A

Insoluble, metabolically unreactive. Principally structured:
Collagen
Keratin (skin hair nails fur and wool)
Fibrin (blood clots)
Elastin (elastic fibres of connective tissues eg arterial walls)
Myosin (muscle)

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13
Q

Physical structure of collagen triple helix

A

Glycine, hydrophone, proline

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14
Q

Fibrous proteins

A

Insoluble, metabolically unreactive. Principally structural proteins:
Collagen
Keratin (skin hair nails fur wool)
Elastin (elastic fibres of connective tissue eg arterial walls)
Myosin (muscle)

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15
Q

Globular proteins

A

Spherical. Backbone folds on itself. Water-soluble compact

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16
Q

Globular proteins structure

A

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

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17
Q

Sterols examples

A

Cortisol, Cholesterol, Estrogen (estradiol) , testosterone

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18
Q

Fatty acids (acyl lipids)

A

Degree of saturation affects van der Waals forces which change lipid physical boundaries

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19
Q

Stearic acid (saturated fat and fatty acid)

A

at room temperature the molecules are tightly packed forming a solid

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20
Q

Unsaturated fat and fatty acids (oleic acid)

A

The molecules cannot pack together closely due to kinks in fatty acid tails (cis double bond)

21
Q

Myoglobin

A

Oxygen storage in muscle. Globular, associated with 3• structures. No beta pleated sheet regions, 8 helical regions (75 percent of all aa), single chain (153 aa), random coiling

22
Q

Absence of haem group in myoglobin

A

Forms apoprotein which is not as tightly folded

23
Q

Myoglobin interior

A

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

24
Q

Prosthetic haem group

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

25
Q

Haemoglobin

A

Oxygen transport. 4• structures. 2 pairs of polypeptide chains (2a and 2b) folded in a shape similar to myoglobin. Spheroidal. Four haem groups lie on surface in individual pockets far apart

26
Q

Haemoglobin a and b chain

A

A chain = 141
B chain = 146

27
Q

Interactions Haemoglobin

A

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

28
Q

Irregular shape

A

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

29
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

30
Q

Hormone

A

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

31
Q

Hormones can be

A

Proteins polypeptide amino acid derivatives or steroids

32
Q

Enzymes

A

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

33
Q

Muscle contraction

A

Myosin (fibrous)

Actin (gobular)

34
Q

Immune protection

A

Antibodies, cytokines

35
Q

Monosaccharides

A

The building blocks of more complex carbohydrates

36
Q

Aldoses vs ketoses

A

Aldoses contain aldehyde group and ketoses contain ketone group

37
Q

Starch vs cellulose

A

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

38
Q

Disacchardides

A

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

39
Q

Glucose plus glucose

A

Maltose

40
Q

Sucrose plus maltose

A

Lactose

41
Q

Difference between alpha and beta configuration

A

OH in alpha below 1 and above 1 in beta

42
Q

Starch vs cellulose up or down

A

Starch down but cellulose up

43
Q

Amylose

A

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

44
Q

Amylopectin

A

Branched glucose units (up to 50,000) 30 a-1,4-linked units until branch point (a-1,6 link)
Food reserve

45
Q

Glycogen

A

Same structure as starch but more highly branched
Food reserve

46
Q

Cellulose

A

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

47
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

48
Q

Glycerides (based on glycerol)

A

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