biological molecules Flashcards

(51 cards)

1
Q

what is a monomer

A

small units from which a larger units are made from

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2
Q

what is a polymer

A

molecules made from a large number of monomers joined together

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3
Q

give an example of a monomer

A

monosaccharides-glucose, fructose or galactose
amino acids
nucleotides

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4
Q

give an example of a polymer

A

protein
starch
DNA

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5
Q

what is a condensation reaction

A

joining of 2 molecules with the formation pf a chemical bond and involves water as a bi-product

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6
Q

what is an example of a condensation reaction

A

glucose+fructose=sucrose+water
glucose+glucose=maltose+water
galactose+glucose=lactose+water

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7
Q

what is a hydrolysis reaction

A

breaking of a chemical bonds between 2 molecules and involves the use of a water molecules

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8
Q

what is an example of a hydrolysis reaction

A

lactose+water=galactose+glucose

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9
Q

what is an organic molecule

A

carbon containing molecules made up of:
-carbon
-hydrogen
-oxygen
-nitrogen

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10
Q

what are the 6 types of bonds, explain their formation and use

A

ionic-attraction between opposite charges- fairly strong cell membranes
disulphide- occurs during protein folding- stabilises protein/ catalyst
hydrogen- H+ ion- cellulose, b-sheets and DNA- very weak
ester- condensation reactions in lipids- 3 on tri- 2 on phos
peptide- condensation in proteins- one acid to carboxyl group
glycosidic- condensation of a-glucose and b-glucose- 1-4 and 1-6 bonds

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11
Q

explain how to do a test for reducing sugars

A
  1. 1cm3 of sample to a test tube
  2. add a few drops of Benedict’s solution
    3.shake to mix
  3. heat in boiling water form 5 minutes
  4. postive = blue to either green if its a low conc or red if a high conc
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12
Q

why does the Benedict solution change colour if its a reducing sugar

A

it has one carbon available which means it can donate electrons(reduce) to turn the colour

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13
Q

describe the test for non-reducing sugars

A

if non-reducing the benedicts won’t change colour so use this:
1. add 1cm3 of dilute hydrochloric acid to the test sample
2. gently place it into boiling water for 5 minutes
3. neutralise with sodium hydrocarbonate powder (test with ph strip)
4. do the Benedict’s test

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14
Q

describe the test for lipids

A
  1. add 2cm3 of sample into test tube
  2. add 5cm3 of ethanol
    3.place bung in and mix then allow it to settle
  3. pour the contense of the test tube into 5cm3 of distilled water
  4. if it is cloudy white it contains lipids
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15
Q

what should you always do before the emulsion test

A
  1. if sample is solid mix with ethanol or alcohol
  2. ensure test tubes are dry and clean
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16
Q

describe the test for starch

A
  1. add 2cm3 of test solution to a test tube
  2. add several drops of dilute iodine
    3.shake to mix
  3. positive result is brown to blue/black
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17
Q

describe the test for proteins

A
  1. prepare your sample
  2. add a few drops of Biuret solution
    3.shake to mix
  3. its positive if colour changes from blue to purple/violet
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18
Q

can you draw alpha glucose

A

CH2OH
H I________O H
I / |
OH \____________/OH
H. OH

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19
Q

can you draw beta glucose

A

CH2OH
OH I________O OH
I / |
H \____________/ H
H. OH

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20
Q

can you draw a condensation reaction

A

look up if you cant

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21
Q

what type of bond is formed between glucose

22
Q

what is starch used for

A

energy store in plants

23
Q

describe amylose

A
  • 1-4 glycosidic bonds
  • unbranched
    -helical to allow it to be compact
24
Q

describe amylopectin

A
  • important to hydrolyse
  • has a 1-6 glycosidic bond
    -has branches
  • has a few 1-4 bonds
25
what are the properties of starch
insoluble- doesn't affect water potential large- doesn't move out of the cell -made from a-glucose so quick release energy - branches allow rapid hydrolysis
26
what is the function of glycogen
quick release energy
27
what are so properties of glycogen
- made of a-glucose - it has a 1-4 and 1-6 glycosidic bonds - its branched and helical - compact - bonding makes it able to do its job
28
how is glycogen broken down
respiration or hydrolyses
29
what is the function of cellulose
strengthen cell walls
30
what are the properties of cellulose
- made from b glucose -forms microfibrils - has hydrogen bonds in between each layer which makes it collectively strong -its insoluble but allows water through osmosis - it has 1-4 glycosidic bonds
31
draw a cellulose molecule
each b-glucose molecule is inverted each time
31
what are the two types of lipids
phospholipids triglycerides
32
what are some common traits off lipids
- each contain carbon, hydrogen and oxygen -they are insoluble but sometimes soluble in alcohol - made of glycerol and fatty acids
33
what is the difference between a saturated and unsaturated lipid
saturated has no double bonds between carbon and can be compact unsaturated has a double bond between carbon
34
what are the 2 types of unsaturated molecules
mono-unsaturated- single double bond poly-unsaturated- has more than one double bond
35
what is a triglyceride made of
1 glycerol 3 fatty acids
36
what type of bond does a lipid form
an ester
37
draw the formation of a triglyceride
look at notes
38
draw an unsaturated and saturated lipid
look at notes
39
what are the properties of triglycerides
-strong- lots of bonds -lightweight- compact - large -insoluble - non polar - releases water when oxidised
40
what is a phosopholipid made of
-phosphate head - glycerol - 2 fatty acid
41
how does a phospholipid use its hydrophilic head
it is used to create cell membranes as they form two layers where they attract water outside and inside this creates a layer
42
how does a phospholipid use its hydrophilic tail
it creates a bilayer plasma- the tail is used to protect vital hormones from water as it repels them
43
what is a protein used for
make up most things in the body- big 3D molecules
44
what is the sequence for proteins
amino acids -> peptide -> polypeptide
45
how many amino acids are their in the body
20
46
what is the first stage sequence
amino acids
47
what are the two groups in an amino acid
amino group carboxylic group
48
draw an amino acid
look at notes
49
Name and describe the 5 stages of protein production
Amino acids Primary - the sequence of amino acids in the polypeptide chain- determines shape/ function Secondary- the chain is then folded into either a a-helix or a b-pleated sheet Tertiary- once secondary is formed the molecule folds into a 3d shape- here it makes the 3 types of bonds ionic hydrogen and disulphide. Quaternary- multiple protein molecules bind together to form a protein
50
What are the 2 types of tertiary structure
Globular- carries out metabolic function Fibrosis- long chains which run Parallel to another these are linked by cross bridge