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Biology AS > 1A- Biological molecules > Flashcards

1A- Biological molecules Flashcards

1
Q

Carbohydrates uses

A

1-respiratory substrates

2-structural components in plasma membranes and cell walls

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2
Q

Lipids uses

A

1-bilayer of plasma membranes
2-hormones
3-respiratory substrate

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3
Q

Proteins uses

A

1-enzymes
2-chemical messengers
3-DNA and RNA

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4
Q

Monomers

A

Small, basic molecular unit chemically bonded together to form polymers via condensation reaction

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5
Q

Polymer

A

large complex molecule composed of chemically bonded monomers bonded by condensation reaction

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6
Q

Condensation reation

A

forms a chemical bond between monomers and releasing a water molecule

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7
Q

Hydrolysis reaction

A

Breaks/ hydrolyse the chemical bonds between monomers using a water molecule

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8
Q

Monosaccharides

A

Monomers which form glycosidic bonds to form polysaccharides via condensation reactions

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9
Q

alpha glucose structure

A

H above OH

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10
Q

Beta glucose

A

OH above H

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11
Q

Disaccharides

A

2 monosaccharides which form a glycosidic bonds via condensation reactions

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12
Q

Maltose disaccharides

A

2 glucose

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13
Q

sucrose disaccharides

A

glucose and fructose

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14
Q

lactose disaccharides

A

glucose and Galactose

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15
Q

Benedicts test for Reducing sugars

A

1-benedicts reagent and heated in hot water bath
Negative= stays blue
Positives= green yellow orange brick-red precipitate
2- The higher the conc of reducing sugar, further the colour change
3- filter and weigh precipitate and use calorimeter to measure absorbance of benedicts reagents

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16
Q

Benedicts test for Non-reducing sugars

A

1-add HCl and heat in water bath
2-add dilute hydrogen carbonate to neutralise
3- carry out benedicts test

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17
Q

Polysaccharides

A

2 monosaccharides chemically join by glycosidic bonds via condensation reaction

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18
Q

Iodine test for starch

A

1-iodine dissolved in potassium iodide solution
2-Positive= stays browny-orange
3-negative= dark blue-black

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19
Q

Starch properties

A

1- insoluble in water so doesnt affect water potential so water doesnt enter via osmosis causing cell to swell
2-large molecule cant leave cell- good energy storage
3- compact-lots energy stored in small space

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20
Q

Amylose

A

1-long unbranched polysaccharide chain of alpha glucose joined by glycosidic bonds via condensation reactions
2-alpha helix structure= H bonds
3-compact-fit more in a space

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21
Q

Amylopectin

A

1-long branched polysaccharide chains of alpha glucose joined by glycosidic bonds via condensation reactions
2-side branches= allow enzymes to hydrolyse glycosidic bonds
3-glucose released easily for repiration

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22
Q

Glycogen

A

1-long, branched polysaccharide chains of alpha glucose
2-lots of side branches, enzymes hydrolyse glycosidic bonds and release energy quickly
3- compact good for energy storage

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23
Q

Cellulose

A 
1-long, unbranched polysaccharide chains of beta glucose linked via glysoidic bonds 
2-straight cellulose chains
3-cellulose chains linked by H bonds
4- strong microfibrils structure
5-structural support for cells
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24
Q

Triglycerides structure

A

1-glycerol bonded to 3 fatty acids
2-ester bond
3-fatty acid HC tails hydrophobic

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25
Q

Triglyceride formation

A

1-Condensation reaction forms ester bond between glycerol and 3 fatty acids chains releasing H2O molecules

26
Q

Phospholipids

A

Glycerol, 2 fatty acids joined by ester bonds and phosphate group

27
Q

Why storage molecules are insoluble

A

So they don’t dissolve in water

28
Q

Triglycerides Properties

A

1-energy storage-long HC tails of fatty acids contain lots of chemical energy
2-insoluble in water so don’t affect water potential as water doesn’t enter via osmosis and cause cell to swell
3-Bundle together to form insoluble droplets in cells

29
Q

Phospholipids properties

A

1-bilayer on cell membranes control what enter cell
2-Hydrophilic head=phosphate
3-Hydrophobic= fatty acid tails
4-water soluble substances can’t easily pass through

30
Q

emulsion tests for lipids

A

1-ethanol and shake for 1 mins
2- add water
positive= cloudy milky white solution
the more lipid the more milky

31
Q

protein bonds

A

peptide bonds

32
Q

Dipeptide and Polypeptide

A

-condensation reactions between amino acids form pepetide bonds and releases water

33
Q

Primary structure

A

-sequence of amino acids joined by peptide bonds in a polypeptide chain

34
Q

Secondary Structure

A
  • H bonds form between amino acids in polypeptide chain

- alpha helix and beta pleated sheet

35
Q

Tertiary structure

A

1-Polypeptide chain coiled and folded further
2-More H bonds form
3- Ionic bonds
4-Disulfide bridges (covalent) between cysteine and sulphur
5-final 3d structure for single polynucleotide chain

36
Q

Quaternary Structure

A

1-The way several different polypeptide chains held by H, Ionic and disulfide bridges are together
2-Proteins final 3D structure for Proteins with more than 1 polypeptide chains

37
Q

Biuret test for proteins

A

1-add NaOH to neutralise
2-add copper(ii) sulphate solution
Positive=goes purple
Negative=stays blue

38
Q

Proteins function determined by

A

shape and structure

39
Q

Structural Proteins

A
  • Physically strong
  • long polypeptide chains parallel with cross-links between
  • Quaternary structure
40
Q

Transport Proteins

A
  • Channel proteins contain hydrophobic and hydrophillic amino acids that cause protein to fold and form a channel
  • Quaternary structure
41
Q

Antibodies proteins

A
  • immune response
  • made of 2 light polypeptide chains and 2 heavy polypeptide chains
  • variable regions with variable amino acid sequences
42
Q

Enzymes proteins

A
  • spherical due to tight folding of polypeptide chains

- soluble

43
Q

Hb properties

A
  • compact
  • soluble
  • easy to transport O2 around body
44
Q

Protein uses

A 
1-Enzymes
2-Antibodies
3-Transport Proteins
4-Structural proteins 
5-Chemical messengers
45
Q

Enzyme

A

1- protein catalyses metabolic reaction by lowering the activation energy on a cellular and a molecular level, icreasing the rate of a reaction without being used up
2- has active site, specific shape, sepcific tertiary structure
3-E-S complex

46
Q

How E-S complex lowers activation energy by

A

1-Enzyme active site holds 2 substrates together, reducing repulsion between substrate so bond easily
2-Enzyme active site puts strain on bonds in 2 substrates so breaks up easily

47
Q

Induced fit model

A

1-active site has specific shape due to specific tertiary structure of H, ionic and disulfide bridges of polypepide
2-complementry E-S complex
3-substrate causes active site to change shape
4-active site turn back to original shape

48
Q

why lock and key theory is no longer accepted

A

doesn’t show how active site slightly changes shape to bind to substrate

49
Q

enzyme properties determined by

A

1-Tertiary structure

50
Q

enzyme properties

A

1-specific only catalyse 1 reaction= complementry active site to a specific substrate
2-active site varies
3- tertiary structure altered- active site changes
4-primary structure of protein-determined by gene- if mutation occurs changes tertiary structure

51
Q

factors affecting enzyme reaction

A

1-temp
2-pH
3-substrate conc
4-enzyme conc

52
Q

How to measure enzyme activity / rate of reaction

A

1- How fast product is made-measure amount of product at different times
2-How fast substrate is broken down- measure substrate left at different times

53
Q

Temperature affect on enzymes

A

1-Rate Increases as Temp Increases- more kinetic energy, molecules move faster, substrates more likely to collide with active site enzyme
2- Too high, vibrations increase, break bonds in tertiary structure, active site changes shape, denatures permanently somethimes enzyme, no E-S complex,rate decreases
3-optimum temp, fastest reaction rate

54
Q

pH affect on enzymes

A

1- Above and below optimum pH- H+ and OH- disrupt H and ionic bonds, alters tertiary structure, acitve site changes shape, denatures, rate decreases

55
Q

Substrate conc affect on enzyme

A

1- Higher substrate conc, faster rate, more likely collisions between E and S, more active sites occupied
2- Until saturation point- all acitve sites occupied- plateau graph- increasing substrate conc has no effect so constant rate

56
Q

Enzyme conc affect on enzyme

A

1-Increase enzyme, more likely collisions, form complementary E-S complex, increases rate
2-Amount of substrate limited,- adding more has no affect until enzyme conc increases too

57
Q

competitive inhibitor

A

1-same shape as substrate, compete with molecules and block active site so no substrate binds
2-High conc of inhibitor, blocks active site, less active sites saturated by substrate- decreases reaction rate
3-High conc of substrate- substrate chance of getting to active site before inhibitor increase-increasing conc of substrate, increases reaction rate- competaive inhibitor out competed

58
Q

Non competitive inhibitor

A

1-bind away from active site which changes shape, No complementary E-S complex formed, rate decreases
2- don’t compete with substrate to bind to active site due to different shapes, less active sites saturated rate decreases
3-increasing substrate- no effect

59
Q

saturation point

A

when all the active sites are occupied

60
Q

when graph plateaus

A

-reaction rate constant for substrate conc and enzyme conc

61
Q

how do fatty acids and glycerol enter cell

A

-diffusion

62
Q

starch

A

-mixture of 2 alpha glucose polysacchaides amylopectin and amylose
-Amylose = 1-long unbranched polysaccharide chain of alpha glucose joined by glycosidic bonds via condensation reactions
2-alpha helix structure= H bonds
3-compact-fit more in a space
-Amylopectin= 1-long branched polysaccharide chains of alpha glucose joined by glycosidic bonds via condensation reactions
2-side branches= allow enzymes to hydrolyse glycosidic bonds
3-glucose released easily for repiration

Biology AS (11 decks)

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