Biomolecules Flashcards

(45 cards)

1
Q

Biological washing powders often contain a number of different enzymes. This enables them to remove a wider range of stains from clothes. Explain why a number of enzymes are requires to remove a wider range of stains
(General enzyme question layout)

A

Stains caused by different substances
Enzymes are specific
Active site specific to substrate/ other substances cannot fit active site

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2
Q

Different sequences of bases code for different proteins explain how

A

Protein made of chain of amino acids
Each amino acid has its own base/ triplet code

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3
Q

Monosaccharides

A

(CH2O)n
Soluble

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4
Q

reducing sugars

A

All monosaccharides and some disaccharides (maltose)
Can donate electrons to another chemical (reduces that chemical)

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5
Q

Test for reducing sugars

A

Add Benedict’s reagent to sample
Heat in water bath that’s being brought to the boil
+ will form coloured precipitate (red copper 1 oxide)

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6
Q

Benedict’s solution

A

Alkaline solution of copper (ll) sulfate
Reduced by reducing sugars to produce copper (l) oxide (red)

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7
Q

Semi quantitative use of Benedict’s test

A

Estimate the approximate amount of reducing sugar in sample as colour of precipitate depends on concentrations of sugar

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8
Q

More accurate method for Benedict’s test

A

Filter the solution and weigh the precipitate

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9
Q

Test for non reducing sugars

A

New sample, add dilute HCl (breaks down into monosaccharides by hydrolysis) and heat in water bath brought to boil
Add sodium hydrogencarbonate to neutralise it (Benedict’s reagent doesn’t work in acidic conditions) test with pH paper to check solution is alkaline
Add Benedict’s solution and heat in water bath brought to boil
+ coloured precipitate

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10
Q

Alpha glucose

A

OH at bottom

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11
Q

Solubility of polysaccharides

A

Insoluble

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12
Q

Starch

A

Plant cells
Small granules/ grains
(Long)Chains may be branched or unbranched, the unbranched chain (amylose) is wound into a tight coil to make the molecule compact. Branched chain (amylopectin) has many ends which can be acted in by enzymes simultaneously so glucose monomers are released rapidly and can be easily transported and readily used.
Insoluble so doesn’t affect water potential
Large and insoluble do doesn’t diffuse out of cells
Compact, lots stored in small space

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13
Q

Test for starch

A

Add iodine in potassium iodide solution to sample
+ blue black

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14
Q

Glycogen

A

Animals and bacteria
Shorter chains than starch and more branched
Stored as small granules mainly in the muscle and liver
Insoluble so doesn’t affect water potential and doesn’t diffuse out of cells
Compact
Highly branched (higher metabolic rate than plants)

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15
Q

Cellulose

A

Straight unbranched long chain
Run parallel to each other, allowing hydrogen bonds to form cross linkages between adjacent chains (collective strength)
Cellulose molecules grouped together to form microfibrils, then fibres
Provides rigidity
Turgid- exerts an inward pressure that stops any further influx of water. Also provides maximum surface area for photosynthesis

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16
Q

Lipids

A

CHO
Insoluble in water
Soluble in organic solvents
Energy source when oxidised
Waterproofing (waxy lipid cuticles on plants and insects and mammals produce oily secretions from glands in skin)
Insulation (slow conductors of heat so retain heat, electrical insulators)
Protection (stored around delicate organs like kidneys)

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17
Q

Fatty acid
Glycerol

A

RCOOH
CH2OH

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18
Q

Triglycerides

A

High ratio of energy storing carbon hydrogen bonds to carbon atoms and are therefore an excellent source of energy
Low mass to energy ratio
Insoluble as large and non polar
High ratio of hydrogen to oxygen atoms so release water when oxidised (water source)

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19
Q

Phospholipids

A

Phosphate molecule
Amphiphilic
Polar so form a bilayer in aqueous environments
Can form glycolipids by combining with carbohydrates within the cell surface membrane, for cell recognition
Provide flexibility to membrane

20
Q

Emulsion test for lipids

A

Add ethanol to sample then shake
Add water then shake
Milky emulsion

21
Q

Explanation of emulsion

A

Lipid in the sample is finely dispersed in the water to form an emulsion
Light passing through the emulsion is refracted as it passes from oil to water droplets ( cloudy)

22
Q

Amino acids as indirect evidence for evolution

A

The same 20 amino acids occur in all living organisms, different only in their side groups

23
Q

Formation of peptide bond

A

OH from carboxyl group
H from amine group

24
Q

Secondary structure of a protein

A

H on NH has overall + and O on C=O has - so from weak hydrogen bonds causing chain to twist and fold into a 3D shape

25
Tertiary structure of a polypeptide
Further twisting and folding Hydrogen bonds, easily broken Ionic bonds- form between carboxyl and amino groups. Easily broken by changes in pH Disulfide bridges- strong, between two cysteine amino acids (bond between 2 sulfur atoms)
26
Biuret test for proteins
Add sodium hydroxide to sample Add dilute copper (ll) sulfate solution + purple - blue (Can just say biuret reagent)
27
Enzymes
Spherical due to tight folding of polypeptide chains Soluble Roles in metabolism
28
Antibodies
Two short and two long polypeptide chains bonded together Variable regions
29
Transport proteins
Channel proteins- contain hydrophobic and hydrophilic amino acids which cause the protein to fold up and form a channel Transport molecules and ions across the membrane
30
Structural proteins
Long polypeptide chains lying parallel to each other with cross links between them Physically strong Keratin (hair and nails) Collagen (connective tissue)
31
Induced fit model
Active site forms as the enzyme and substrate interact The enzyme is flexible and can mould itself around the substrate The enzyme has a certain general shape but this alters in the presence of the substrate As it changes shape the enzyme puts a strain on the substrate molecule which distorts a particular bond or bonds in the substrate and consequently lowers the activation energy needed to break that bond
32
Lock and key mechanism
Shape of substrate (key) exactly fits the active site of the enzyme (lock) Enzyme has a rigid structure
33
Effect of increased temperature on enzyme reaction
Increases kinetic energy of the molecules— more frequent and successful collisions Causes hydrogen and ionic bonds to break, substrate less able to form complex Denatured
34
Effect of pH on enzyme action
Change in pH alters the charges on the amino acids that make up the active site of the enzyme so alters active site Affects hydrogen and ionic bonding
35
Calculating pH with hydrogen ion concentration
pH= -log10[H+]
36
Effect of enzyme concentration on enzyme action
More frequent collisions Proportionate increase long as there is excess substrate Until amount of substrate is limited and graph levels off
37
Effect of increasing substrate concentration on rate of enzyme action
More frequent collisions so proportional increase Until saturation point when all active sites are full Rate will decrease over time too if no more substrate is being added
38
Competitive inhibitors
Have a molecular shape similar to that of the substrate Occupy active site of enzyme, no reaction occurs and eventually detaches Block- substrate must compete with the inhibitor If substrate concentration is increased then the effect of the inhibitor is reduced All substrates will eventually occupy active site
39
Non competitive inhibition
Bind to enzyme at a site that isn’t the active site Alters shape of active site so that substrate molecules can no longer occupy it Increase in substrate concentration has no effect on the inhibitor
40
Measuring enzyme catalysed reactions
Formation of products or loss of substrate 1. Lots of substrate so easy for enzyme substrate complexes to form 2. Amount of substrate decreases as its broken down and amount of product increases 3. More difficult for substrate to bind to enzyme as there are fewer substrate molecules and product molecules get in the way so rate increases at decreasing rate 4. Graph flattens when all substrate has been broken down into product
41
Measuring amount of a gas produced to measure rate of reaction
Upside down measuring cylinder in trough of water, connected with a delivery tube to a boiling tube sealed with a bung Add buffer solution to boiling tube to keep pH constant Fill each boiling tube with equal volumes and concentrations of the solution Put each boiling tube in a water bath set to different temperatures along with another tube of catalase Use pipette to add same volume of set concentration of catalase to each boiling tube and replace bung Time oxygen production Repeat at each temp 3 times to get average volume of oxygen produced Calculate average rate if reaction at each temp
42
Measuring how fast a substrate is broken down
Drop of iodine in potassium iodide added to each well in spotting tile Known concentration of starch and amylase added to test tube Dropping pipette to add this to a well and observe colour change Do this at regular intervals Stop when well remains browny orange Repeat with different concentrations of amylase
43
Altering the methods for other variables
pH- adding buffer solution with different pH to each tube Substrate conc Temp Enzyme conc
44
Position of bands dna replication
“Denser so move further”
45
Use of detergent
Dissolved membranes/ organelles