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1A-Biological Molecules Flashcards

1
Q

Monomer

A

Small basic molecular unit

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2
Q

Polymer

A

Large complex molecule composed of long chains of monomers

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3
Q

Monomer types

A

Amino acid monosaccharides DNA, ATP and RNA nucleotides glycerol and fatty acids

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4
Q

Polymer types

A

Polysaccharides, polynucleotides, Polypeptides,

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5
Q

Condensation reaction

A

Joins to molecules together forming a chemical bond and releasing a Water molecule

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6
Q

Hydrolysis

A

Breaks chemical bond between 2 molecules using a water molecule

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7
Q

Carbohydrates uses

A

Respiratory substrates, Structural components in plasma membranes and cell walls

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8
Q

Lipids uses

A

Respiratory substrates Phospholipid bilayer of plasma membranes Hormones

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9
Q

Proteins uses

A

Enzymes. Chemical messengers. DNA RNA Cells

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10
Q

Monosaccharides

A

Monomers of carbohydrates

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11
Q

Bond in carbohydrates between disaccharides

A

Glycosidic

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12
Q

Maltose disaccharide

A

Glucose and glucose

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13
Q

Sucrose disaccharide

A

Fructose and glucose

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14
Q

Lactose disaccharide

A

Galactose and glucose

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15
Q

Alpha glucose

A

H on top

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16
Q

Beta glucose

A

OH on top

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17
Q

Glycogen and starch formation

A

Condensation of alpha glucose

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18
Q

Cellulose

A

Condensation of beta glucose

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19
Q

Polysaccharide

A

Condensation reaction of more than 2 monosaccharides

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20
Q

Break glycosidic bonds

A

Hydrolysis reaction by adding water splits at O

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21
Q

Amylose

A

1.Starch- long unbranched chain of alpha glucose 2.angles of glycosidic bond =helical structure 3.helical structure = held via H bonds 4.So compact =good for storage

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22
Q

Amylopectin

A

1.Starch-long branched chain of alpha glucose 2.side branches=allow enzymes to break glycosidic bonds easier glucose released

23
Q

Starch properties

A

-Insoluble in water, doesn’t affect WP, no water enters cells via osmosis, no swelling, So good for storage -large molecule can’t leave cell

24
Q

Glycogen an energy store

A

Polysaccharide of alpha glucose. Lots of side branches = glucose release quicker as enzymes have increased surface area to work on so more energy released from energy store . Compact. -good storage of energy

25
Cellulose (in cell walls)
-Long unbranched chain of beta glucose -beta glucose bonded forming straight cellulose chains - linked via H Bonds -form strong microfibrils fibres = provides structural support for cells
26
Iodine test for starch
1-iodine dissolved in potassium iodide solution 2-Positive=dark blue black colour Negative= orange
27
Reducing sugars test
1-Benedict's reagent and heat in boiling hot water bath 2-positive =coloured precipitate green orange brick red - remove precipitate and use calorimeter as high concs of sugar =further colour change
28
Non reducing sugars
1- Test for non if negative /blue result for reducing 2-heat new sample with dilute HCL and neutralise with sodium hydrogen carbonate 3- Benedict's reagent and heat in hw bath
29
Use excess of Benedict's solution
Make sure all solutions of sugar react
30
Lipids
Contain hydrocarbons
31
Triglycerides
1 glycerol attached to 3 fatty acids
32
Bonds in lipids
Ester
33
Formation of triglycerides
Ester bond forms via condensation reaction releasing h2o
34
Phospholipids
1 phosphate molecule attacked to glycerol and 2 fatty acids -phosphate hydrophilic -fatty acids hydrophobic
35
Properties of triglycerides
1-Energy storage molecules= fatty acid tails contain lots of energy 2-insoluble/don't affect WP/no swelling caused by osmosis -form droplets insoluble tails face inwards
36
Phospholipid properties
1-phospholipid Bilayer of cell membranes = hydrophobic fatty acids face in and hydrophilic face out 2.water soluble substances can't pass through it
37
Emulsion test lipids
Shake with ethanol for 1 min add water and cloudy milky emulsion forms
38
Biuret test for proteins
1 NaOH solution 2-copper(II) sulphate solution Positive-purple negative-blue
39
Tertiary structure
-H and ionic bonds +/- molecule parts / disulfide bridges between 2 cysteines sulphur atoms bond -final 3D structure for single polypeptide
40
Quaternary structure
-proteins final 3D structure -more than one polypeptide chain - held by disulfide bridges ionic and H bonds assembled in a specific way
41
Proteins uses
Enzymes antibodies transport and structural proteins
42
How enzymes lower activation energy ?
1 -enzyme holds with substrate together reducing repulsion. 2-active site strains substrates bonds so breaks up easily
43
Induced fit model
-Enzymes active site complementary shape to substrate. -substrate makes enzymes active site change shape forming enzyme-substrate complex
44
Properties of enzymes
Specific Tertiary structure of active site and forms complementary E-S complex due to complementary shape of active site
45
Measuring enzyme activity
1-how fast the product is made 2- how fast substrate is broken down
46
Factors that affect enzymes
1- temperature, 2-pH 3-substrate concentration 4-enzyme concentrations
47
Increasing temperature affect on enzymes
-More kinetic energy faster molecules -substrate molecules more likely to collide with enzymes active site -energy of collisions increases more likely to result in a reaction - faster rate
48
Too much temp increase in enzymes
-enzymes molecules vibrate more -vibration breaks bonds that hold enzymes in shape. -alters shape of active site -active site no longer complementary to enzyme so no E-S complex formed - denatured so no longer a functioning catalyst
49
pH affect on enzyme
-enzymes have different optimum pH. -H+and OH- ions disrupt ionic and hydrogen bonds that hold tertiary structure -active site altered doesn't form complementary E-S complex and enzyme denatured
50
Increase substrate concentration affect on enzymes
-Higher substrate conc the faster the rate of reaction -more likely collisions until saturation point - all active sites taken so no more E-S formed so no affect increasing amount of substrate more
51
Enzyme concentration affect
More enzymes faster reaction as more likely to collide + form E-S complex- until all substrates form E-S where increasing the enzymes has no further affect on rate
52
Competitive inhibitors
-Similar shape to substrate so form complementary E-S complexes with enzymes and block it so no reactions. -compete with substrate for active site
53
Non competitive inhibitor
Bond to enzyme away from it active site causing active site to change shape so no more E-S complex formed decreasing rate of reaction as no longer complementary - don't compete with substrate so increasing substrate -no effect

Biology AS (11 decks)

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