Biological Molecules Flashcards

(33 cards)

1
Q

Glucose + glucose

A

Maltose + H2O

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2
Q

Glucose + galactose

A

Lactose + H2O

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3
Q

Glucose + fructose

A

Sucrose + H2O

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4
Q

Properties of starch

A

Large - cannot cross cell surface membrane
Insoluble - osmotically inactive
Helical - forms a compact store
Branched - glucose is easily released

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5
Q

Properties of glycogen

A

Insoluble - osmotically inactive
Branched - for easy release of glucose

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6
Q

Test for reducing sugars

A

Benedict’s test

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7
Q

Benedict’s test method

A

Add sample to same volume of Benedict’s solution
Heat to 95° in a water bath

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8
Q

Test for starch

A

Iodine test

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9
Q

Positive result of starch test

A

Colour change
Orange —> blue/ black

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10
Q

Positive result of Benedict’s test

A

Colour change
Blue —> brick red

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11
Q

Test for protein

A

Biurets test

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12
Q

Positive result for biurets test

A

Colour change
Blue —> lilac

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13
Q

Test for lipids

A

Emulsion test

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14
Q

Emulsion test method

A

Place sample in test tube with ethanol
Shake mixture so fat dissolves
Add water and mix

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15
Q

Positive result for emulsion test

A

White emulsion forms

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16
Q

Method for testing non reducing sugar

A

Carry out Benedict’s test on sample - negative result

Heat sample in water bath to 95° with HCl
Let cool
Neutralise with alkali
Add Benedict’s solution and heat in water bath to 95°
Positive result shows none reducing sugar present

17
Q

Alpha glucose

18
Q

Condensation reaction with peptides

19
Q

What bond joins amino acids

A

Peptide bonds as a result of a condensation reaction

20
Q

What bonds join phospholipids

A

Esther bonds as a result of a condensation reaction

21
Q

What bonds join monosaccharides

A

Glycosidic bonds as a result of condensation reactions

22
Q

Primary structure of proteins

A

Sequence of amino acids in a polypeptide chain

23
Q

Secondary structure of proteins

A

Coiling/ folding of the polypeptide chain due to hydrogen bonding

Form either alpha helix or beta pleated sheets

24
Q

Tertiary structure of a protein

A

Further coiling / folding of polypeptide chain due
Ionic bonds form
Disulphide bridges form

25
Quaternary structure of proteins
Proteins with more than one polypeptide chain due Ionic
26
Properties of water (4)
Metabolic reactions - metabolite Solvent -transport nutrients -remove waste products Temperature regulation -high heat capacity Absorbs lots of heat energy before temperature increases -large latent heat of vaporisation Cooling effect Support - internal cohesive forces between molecules Supports water tubes eg. Xylem -external cohesive forces provide surface tension -not easily compressed
27
Induced fit enzyme
Active site of enzyme is flexible Presence of specific substrate induces a change in active site shape Active site becomes complementary Enzyme remains unchanged at end of reaction
28
Effect of pH on enzymes
Small optimum pH window Too high or too low pH can denature enzymes Active site changes shape due to change in tertiary structure
29
Effect of temperature on enzymes
Higher temp more kinetic energy Increases frequency of collisions between active site and substrate (more enzyme-substrate complexes) Too high temp can denature enzymes by changing active site shape by altering tertiary structure
30
Competitive inhibition
Inhibitor has a similar structure to substrate and competes to attach to active site Substrate cannot bind RoR decreases Addition of more substrate can increase RoR
31
Non-competitive inhibition
Inhibitor doesn’t have similar structure to substrate Combines elsewhere on the enzyme - not the active site Enzyme inhibitor complex forms Alters tertiary structure of enzyme Substrate cannot bind as it’s no longer complementary
32
ATP
ATP is hydrolysed to release energy and then resynthesized ATP (+atp hydrolyse) —> ADP +Pi
33
ATP
ATP is hydrolysed to release energy and then resynthesized ATP (+atp hydrolyse) —> ADP +Pi