biochemistry Flashcards

(75 cards)

1
Q

what is the other name for proteins? and what does this mean?

A

polypeptides- many amino acids

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

how many amino acids do we have?

A

20

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

how many essential amino acids and what does this mean?

A

9 essential- need to eat, we cannot make

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

ow many non-essential amino acids and what does this mean?

A

11 non-essential- body makes

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

how are amino acids joined?

A

by a condensation polymerisation reaction which forms a repeating backbone with alternating R groups.

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

chirality?

A

amino acids have a chiral carbon centre which means that the have 4 different environments all around- an amine, R, H, carboxy

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

what are the exceptions in amino acids?

A

glycine is not chiral

proline changes from the general structure (but still chiral)n

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

what is the basic end? acidic end?

A
  • amine

- carboxy

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

how are amino acids categorised?

A

by the properties of the R group

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

non-polar

A

dispersion forces only

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

+ charge

A

has an NH3+, NH2+ or NH+

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

polar

A

has an OH, C=O

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

lost some H forming O-

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

what does it mean that amino acids can acid as buffers?

A

they have amphiprotic capacity- act as an acid or base, this leads to conjugate pairs

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

what aspects does a zwitterion have?

A

a positive (protonated) and negative (deprotinated) end

  • neutral overall
  • protonated end is basic and accepts H+ in acidic solutions
  • deprotinated end is acidic and donates H+ in basic solutions
  • therefore amphiprotic and acts as a buffer
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

important note in buffering?

A

R groups can participate

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

at pH 7?

A

always zwitterions because neutral

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

how are dipeptides formed?

A

water is expelled, allowing C=ONH (amide link or peptide link) to form

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

what if dipeptides are being broken down?

A

add water ands its hydrolysis

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

number of waters lost?

A

number of amino acids-1

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

working out number of possibilities

A

use factorials

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

how does hydrolysis work?

A

water is added, the amide link breaks

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

primary structure

A

bead chain of amino acids

- peptide bonds (covalent bonds)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

secondary structure

A

hydrogen bonding occurs causing folding on b-sheet or a-helix

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
tertiary structure
- 4 different types of bonds (governed by R groups) - dispersion - ionic (charges) - hydrogen - disulphide (S-S) order of strength
26
quaternary structure
- when more than one pp chain join together eg. ribosomes, antibodies, haemoglobin
27
protein function
``` structure- keratin transport- Hb toxins defence, immunology- antibodies enzymes- biological catalysts ```
28
what are enzymes and what do they do?
speed up reactions by lowering activation energy needed to break reactant bonds. this leads to energy conservation (more energy put into increasing collisions) and therefore ensures another energy pathway to be present
29
what does it mean that enzymes are specific?
an enzyme only functions on a specific substrate. this is linked to their 3D structure and active site (Complementary bonding)
30
how does the lock and key model work?
when the substrate (key) internal bonds releax, the activation energy is decreased and therefore bonds break more easily
31
enzymes can be reused
they are not consumed by a reaction
32
enzyme-substrate complex
when lock and key fuse
33
induced fit model
active site is modified to better fit the substrate
34
what are the set conditions under which enzymes function?
optimal conditions- pH and temperature | changes to these change bond types and disrupt 3D structure
35
less than optimum temperature
decrease kinetic energy, do not denature (not enough energy) | - hypothermia
36
greater than optimum temperature
denature, 3D structure destroyed, R groups cannot bind, pp chain undone, coagulation (clump) - hyperthermia
37
what are coenzymes formed from?
vitamins we eat
38
what do many coenzymes work?
with a cofactor
39
what are cofactors?
metal ions (cations) or small organic molecules (not proteins)
40
what is 1 coenzyme function?
attach functional groups to the substrate- phosphorylation or methylation - cofactor, coenzyme and substrate bind and coenzyme passed functional group onto the substrate
41
what is 2 coenzyme function?
carry electrons - oxidation and reduction - NAD+ and H+ and 2e- form NADH - same with FAD+ - NAD and FAD are both oxidants
42
how does a coenzyme differ to an enzyme?
a coenzyme needs a cofactor to function
43
how does a cofactor work?
the coenzyme is inactive but when a cofactor binds, it becomes activated and can then bind to the substrate
44
what are carbohydrates made of?
CHO
45
what is the equation of carbohydrates?
Cx(H2O)y where x and y are equal
46
what are carbohydrates a source of?
energy
47
what are the three groups of carbohydrates?
- monosaccharides - disaccharides - polysaccharides
48
what are monosaccharides?
- one sugar - simple sugars - glucose, galactose, fructose glucose and galactose are isomers and hexose fructose is pentose they are highly soluble due to hydrogen bonding
49
what are disaccharides?
- 2 sugars added together - condensation reaction - bind 1 to 4 (horizontal) and water is expelled
50
what are polysaccharides? what are the types?
- many sugars - continued condensation reactions - starch, cellulose, glycogen
51
what is starch? what are the types? how does bonding occur? solubility?
polymer of glucose, stored in plants in the leaves and seeds amylopectin- soluble in water due to its branching structure which exposes OH - has bonding 1 to 4 horizontal and 1 to 6 vertical amylose- insoluble in water as OH are not exposed - only 1 to 4 bonding
52
what is cellulose? humans? bundle parallel?
polymer of beta glucose (humans have alpha). The humans don't have enzymes to break it down, fibre have 1 to 4 bonding and 1 to 6 bonding to form parallel lines
53
what is glycogen? bonding?
a polymer of glucose. it is in excess in humans in liver and muscle cells mainly 1 to 4 bonding (glycosidic linkage) but also some branching with 1 to 6 glycosidic links
54
what are glycosidic links?
C-O-C also called ether links and can be 1 to 4 or 1 to 6
55
how does hydrolysis of sugars occur?
water is added and an enzyme breaks glycosidic link
56
what is GI?
- glycemic index - a way of rating CHO food - rates on affect on Blood Glucose Level over a period of time, namely 2 hours - rates food on how quickly it releases the energy it contains
57
low GI
long time to release energy
58
what is biological availability?
how readily available the energy is in the food we eat
59
what are lipids?
fats | - ester
60
what are triglycerides?
3 glycerol fatty acids (carboxylic acids)
61
how do glycerols and fatty acids form to made a triglyceride?
glycerol and three fatty acids join by condensation reactions, expelling 3 waters and creating an ester link
62
how are triglycerides broken down?
add water
63
polarity of fatty acids? implications?
long hydrocarbon chains that are non-polar. therefore when moving in the blood stream, the lipids need the help of bile
64
what is bile?
a lipoprotein that is a surfactant- chemical that has a non polar nd and a polar end looks like a circle (polar) with a zig zag end (non-polar)
65
how does the fatty acid travel with bile?
in the middle with the polar circles pointing out as they travel through the polar environment
66
what are the physical states of lipids?
solid- butter, lard, wax | liquid- oil
67
what are the chemical structures of lipids?
- saturated: no C=C bond, ane - unsaturated: C=C bond, ene can be polyunsaturated or monounsaturated
68
what do saturated and unsaturated fatty acids look like?
saturated are straight unsaturated have a kink
69
comparing butter and oil?
butter is saturated and therefore has a higher boiling point because with no C=C there are lots of H to engage in dispersion forces and therefore more intermolecular bonding and more energy to overcome oil is unsaturated and has a lower BP. this is because of less H atoms to dispersion force because of double bonds. therefore less energy to overcome and therefore less heat needed to overcome
70
what is the general structure of fatty acids?
alpha end COOH and omega end CH3
71
how do you determine whether a fatty acid is unsaturated and how many C=C bonds it has?
ignore COOH subtract CH3 use CxH2x formula if number of hydrogens is not equal, it is unsaturated subtract hydrogens present from those of CxH2x divide that number by 2 which will give the number of C=C bond
72
what is a cis-fatty acid?
Hs on the same side of the C=C bond and therefore chain has a large kink
73
trans-fatty acid?
Hs are on opposite sides of the C=C bond and there is a smaller kink due to this, they can stack which causes health issues
74
omega 3 fatty acids?
first double bond is on the 3rd carbon from the end
75
omega 6 fatty acid?
the first double bond is on the 6th carbon from the end