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Biology AS > 1A-Biological Molecules > Flashcards

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
Q

Cellulose (in cell walls)

A

-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
Q

Iodine test for starch

A

1-iodine dissolved in potassium iodide solution 2-Positive=dark blue black colour Negative= orange

27
Q

Reducing sugars test

A

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
Q

Non reducing sugars

A

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
Q

Use excess of Benedict’s solution

A

Make sure all solutions of sugar react

30
Q

Lipids

A

Contain hydrocarbons

31
Q

Triglycerides

A

1 glycerol attached to 3 fatty acids

32
Q

Bonds in lipids

A

Ester

33
Q

Formation of triglycerides

A

Ester bond forms via condensation reaction releasing h2o

34
Q

Phospholipids

A

1 phosphate molecule attacked to glycerol and 2 fatty acids -phosphate hydrophilic -fatty acids hydrophobic

35
Q

Properties of triglycerides

A

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
Q

Phospholipid properties

A

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
Q

Emulsion test lipids

A

Shake with ethanol for 1 min add water and cloudy milky emulsion forms

38
Q

Biuret test for proteins

A

1 NaOH solution 2-copper(II) sulphate solution Positive-purple negative-blue

39
Q

Tertiary structure

A

-H and ionic bonds +/- molecule parts / disulfide bridges between 2 cysteines sulphur atoms bond -final 3D structure for single polypeptide

40
Q

Quaternary structure

A

-proteins final 3D structure -more than one polypeptide chain - held by disulfide bridges ionic and H bonds assembled in a specific way

41
Q

Proteins uses

A

Enzymes antibodies transport and structural proteins

42
Q

How enzymes lower activation energy ?

A

1 -enzyme holds with substrate together reducing repulsion. 2-active site strains substrates bonds so breaks up easily

43
Q

Induced fit model

A

-Enzymes active site complementary shape to substrate. -substrate makes enzymes active site change shape forming enzyme-substrate complex

44
Q

Properties of enzymes

A

Specific Tertiary structure of active site and forms complementary E-S complex due to complementary shape of active site

45
Q

Measuring enzyme activity

A

1-how fast the product is made 2- how fast substrate is broken down

46
Q

Factors that affect enzymes

A

1- temperature, 2-pH 3-substrate concentration 4-enzyme concentrations

47
Q

Increasing temperature affect on enzymes

A

-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
Q

Too much temp increase in enzymes

A

-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
Q

pH affect on enzyme

A

-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
Q

Increase substrate concentration affect on enzymes

A

-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
Q

Enzyme concentration affect

A

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
Q

Competitive inhibitors

A

-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
Q

Non competitive inhibitor

A

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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