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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
Triglyceride formation
1-Condensation reaction forms ester bond between glycerol and 3 fatty acids chains releasing H2O molecules
26
Phospholipids
Glycerol, 2 fatty acids joined by ester bonds and phosphate group
27
Why storage molecules are insoluble
So they don't dissolve in water
28
Triglycerides Properties
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
Phospholipids properties
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
emulsion tests for lipids
1-ethanol and shake for 1 mins 2- add water positive= cloudy milky white solution the more lipid the more milky
31
protein bonds
peptide bonds
32
Dipeptide and Polypeptide
-condensation reactions between amino acids form pepetide bonds and releases water
33
Primary structure
-sequence of amino acids joined by peptide bonds in a polypeptide chain
34
Secondary Structure
- H bonds form between amino acids in polypeptide chain | - alpha helix and beta pleated sheet
35
Tertiary structure
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
Quaternary Structure
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
Biuret test for proteins
1-add NaOH to neutralise 2-add copper(ii) sulphate solution Positive=goes purple Negative=stays blue
38
Proteins function determined by
shape and structure
39
Structural Proteins
- Physically strong - long polypeptide chains parallel with cross-links between - Quaternary structure
40
Transport Proteins
- Channel proteins contain hydrophobic and hydrophillic amino acids that cause protein to fold and form a channel - Quaternary structure
41
Antibodies proteins
- immune response - made of 2 light polypeptide chains and 2 heavy polypeptide chains - variable regions with variable amino acid sequences
42
Enzymes proteins
- spherical due to tight folding of polypeptide chains | - soluble
43
Hb properties
- compact - soluble - easy to transport O2 around body
44
Protein uses
``` 1-Enzymes 2-Antibodies 3-Transport Proteins 4-Structural proteins 5-Chemical messengers ```
45
Enzyme
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
How E-S complex lowers activation energy by
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
Induced fit model
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
why lock and key theory is no longer accepted
doesn't show how active site slightly changes shape to bind to substrate
49
enzyme properties determined by
1-Tertiary structure
50
enzyme properties
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
factors affecting enzyme reaction
1-temp 2-pH 3-substrate conc 4-enzyme conc
52
How to measure enzyme activity / rate of reaction
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
Temperature affect on enzymes
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
pH affect on enzymes
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
Substrate conc affect on enzyme
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
Enzyme conc affect on enzyme
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
competitive inhibitor
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
Non competitive inhibitor
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
saturation point
when all the active sites are occupied
60
when graph plateaus
-reaction rate constant for substrate conc and enzyme conc
61
how do fatty acids and glycerol enter cell
-diffusion
62
starch
-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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