Biological Molecules Flashcards

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1
Q

Draw two molecules of alpha glucose and circle where they form a glycosidic bond.

A

OH below the plane
Circle should be around OH group on carbon 1 and 4 from glucose monomers

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2
Q

Describe how you would test for a non-reducing sugar.

A

First add Benedict’s solution and heat to 90C to test for any reducing sugars.
If solution does not change colours non present
Boil with Hydrochloric acid and then sodium hydrogen carbonate to neutralise.
Add Benedict’s and heat to 90C
Should turn dark red in presence of non-reducing sugars

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3
Q

How do you test for presence of a lipid?

A

Add a drop of water, then a drop of ethanol + shake
If a white emulsion is formed it contains lipids.

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4
Q

Describe a method to find the concentration of glucose in an unknown solution.

A

Plot a calibration curve
Prepare known solutions of glucose and add Benedict’s solution to them and place them in a water bath at 90C for 5 minutes.
Filter the precipitate and then add it to a cuvette.
Place into a colorimeter and measure absorbance of green light
Plot these points onto a graph.
Repeat Benedict’s test with unknown solution and then place precipitate into cuvette and measure absorbance of green light.
Read off calibration curve to see concentration of glucose.

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5
Q

Suggest a method other than colorimetry to measure the quantity of reducing sugar in a solution.

A

Add Benedict’s solution and place in water bath at 90C for 5 minutes.
Remove from water bath and filter to remove the precipitate from the solution.
Dry precipitate using heat gun and then measure dry mass as this is proportional to mass of glucose in solution.

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6
Q

Describe and explain the features of starch that make it a good storage molecule

A

Insoluble so doesn’t effect water potential of cell
Coiled into alpha helix so is compact
Branched so more ends for faster enzyme breakdown
Large molecule so cannot cross cell membrane
Polymer of alpha glucose so provides respiratory substrate

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7
Q

Describe and explain two features of cellulose that mean it is adapted to its function.

A

Long straight chains form hydrogen bonds between them to form fibrils which provide strength as structural molecule
Insoluble so does not effect water potential

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8
Q

Describe two differences between the structure of a glycogen and cellulose molecule.

A

Glycogen is Alpha Glucose cellulose is Beta
Cellulose is a straight chain and glycogen is branched
Glycogen is coiled and cellulose is straight
Glycogen has 1-4 and 1-6 but cellulose only has 1-4 glycosidic bonds

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9
Q

Describe how you would test for the presence of a lipid.

A

Add a drop of water
Add ethanol
Shake and a white emulsion is formed

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10
Q

Describe how a triglyceride molecule is formed.

A

Glycerol and three fatty acids
Condensation reaction between each one and removal of three water molecules
Forms an ester bond

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11
Q

Describe the induced fit model of an enzyme.

A

Substrate binds to enzyme active site
Tertiary structure is altered and active site changes slightly and becomes complementary to substrate

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12
Q

Describe how enzymes act as catalysts.

A

Lowers activation energy
Induced fit causes active site to change shapes
So enzyme substrate complex causes bonds to form or break

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13
Q

Describe a biochemical test to test for the presence of proteins in a solution.

A

Add biuret solution + shake
goes from blue to violet/purple

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14
Q

Describe two ways in which all dipeptides are the same and one way in which they are different.

A

Similarities- peptide bond
NH2 at one end
COOH at one end
Two R groups
Differences- different R groups

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15
Q

Describe how a non-competitive inhibitor reduces the rate of an enzyme controlled reaction.

A

Binds to allosteric site of the enzyme
Causes a change in tertiary structure which causes the shape of the active site to change
No longer complementary to substrate so no enzyme-substrate complexes formed

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16
Q

A change from Glycine to Leucine in one position causes no change to protein structure but in another position dramatically reduces rate of reaction. Explain why.

A

Both change negatively charged for positively charged amino acid
In first position it does not change the active site structure.
In second position amino acid was involved in ionic, disulphide or hydrogen bond so tertiary structure and active site shape was changed.

17
Q

Describe the structure of DNA

A

Polymer of nucleotides
Nucleotides made up of deoxyribose, phosphate and nitrogenous base
Phosphodiester bonds between nucleotides
Forms double helix joined by hydrogen bonds
Hydrogen bonding occurs between bases Cytosine + Guanine and Adenine + Thymine

18
Q

Name the protein associated with DNA in a chromosome

A

Histone

19
Q

Describe the function of single stranded DNA fragments and free nucleotides in semi-conservative replication.

A

Single stranded DNA- acts as a template
determines order of nucleotides
Free Nucleotides- line up by complementary base pairing to form new strand

20
Q

Describe three features of DNA and why they are important in DNA replication.

A

Hydrogen bonds are weak- easy to separate so strands can act as templates
Bases line up by complementary base pairing allows accurate replication
Two strands so both can act as templates

21
Q

Contrast the structures of ATP and DNA

A

ATP is ribose, DNA is deoxyribose
ATP contains 3 inorganic phosphates DNA contains one
ATP can only include Adenine but DNA can include Adenine, Guanine, Cytosine or Thymine

22
Q

Explain why DNA polymerase move in opposite directions.

A

DNA strands run antiparallel
Enzymes have a specific tertiary structure which means their active site is complementary to their substrate
Structure of DNA is different on 3’ end and 5’ end
Only complementary to 3’ end so move 5’ -> 3’ on both strands

23
Q

Describe the process of semi conservative replication

A

DNA Helicase breaks hydrogen bonds between DNA strands to leave two template strands
Free nucleotides line up by complementary base pairing
DNA polymerase forms phosphodiester bonds between nucleotides by condensation reaction
DNA polymerase can only move in 5’ to 3’ direction so moves continuously on the leading strand.
On lagging strand it has to detach and reattach further down and Okazaki fragments are joined together by Ligase

24
Q

Describe how ATP is a suitable energy source

A

Releases a small/manageable amount of energy
Can be hydrolysed to release energy instantly
Can be rapidly reformed
Does not leave cells
Can be used to phosphorylate other compounds making them more reactive

25
Q

Describe how ATP is reformed

A

From ADP + Pi
Using ATP synthase
In respiration or photosynthesis

26
Q

Describe how ATP is formed from its components

A

Ribose, phosphate and three Pi
Condensation reaction
Catalysed by ATP synthase

27
Q

Explain 5 properties of water that make it important in an organism

A

Metabolite- in condensation/hydrolysis and photosynthesis/respiration
High specific heat capacity-buffers temperature changes
High Latent heat of vaporisation- provides a cooling effect through evaporation
Cohesion- allows for water to move in a column in plants and surface tension for small insects
Solvent- for transport of substances

28
Q

Describe the roles of iron, sodium and phosphate ions in cells

A

Sodium- used for cotransport of glucose, sodium actively transported out by Na+/K+ pump and creates concentration gradient so diffuses back in associated with glucose
Iron- used in haemoglobin to allows oxygen to bind to be transported
Phosphate- used in DNA nucleotides, hydrophilic part of phospholipid bilayer, used in ATP, used to phosphorylate molecules to make them more reactive