Biological Molecules Flashcards

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
Q

Quaternary structure of proteins

A

Proteins with more than one polypeptide chain due Ionic

26
Q

Properties of water (4)

A

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
Q

Induced fit enzyme

A

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
Q

Effect of pH on enzymes

A

Small optimum pH window
Too high or too low pH can denature enzymes
Active site changes shape due to change in tertiary structure

29
Q

Effect of temperature on enzymes

A

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
Q

Competitive inhibition

A

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
Q

Non-competitive inhibition

A

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
Q

ATP

A

ATP is hydrolysed to release energy and then resynthesized

ATP (+atp hydrolyse) —> ADP +Pi

33
Q

ATP

A

ATP is hydrolysed to release energy and then resynthesized

ATP (+atp hydrolyse) —> ADP +Pi