Bio molecules Flashcards

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1
Q

Metabolism

A

collective chemical processes that take place in an organism

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2
Q

What is maltose composed of?

A

2 glucose

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3
Q

What is sucrose composed of?

A

glucose + fructose

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4
Q

What is lactose composed of?

A

glucose + galactose

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5
Q

Structure + function of glycogen

A
  • highly branched so hydrolysed rapidly -> cope w/ higher metabolic rate of animals
  • insoluble so doesn’t affect water pot.
  • compact -> stored in small space
    => storage of glucose in animals
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6
Q

Structure + function of cellulose

A
  • long straight microfibrils run in parallel creating H bonds between molecules -> strength + rigidity of plant cell wall
  • B glucose alternately rotated 180 creating glycosidic bonds 1’ and 4’ C atoms -> resist osmotic pressure + digestion by enzymes
    => strengthening + maintaining structure of cell wall
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7
Q

Structure + function of starch (amylopectin + amylose)

A
  • amylose has compact helical structure -> efficient storage
  • amylopectin is branched -> easily hydrolysed
  • insoluble -> doesn’t affect water pot.
    => storage of glucose in a plant
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8
Q

Test for reducing sugar

A

Benedict’s solution + heat

blue -> orange/brown if present

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9
Q

Properties of phospholipids

A
  • polar molecule -> in aq. environments forms a bilayer
  • hydrophilic phosphate group helps hold molecule at surface of cell membrane
  • forms glycolipids w/carbs -> cell recognition
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10
Q

Properties of triglycerides

A
  • high ratio of energy storing C-H bonds
  • low mass:energy ratio -> gd for storage
  • insoluble, large -> no effect on water pot.
  • release water when oxidised
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11
Q

Test for lipids

A

Ethanol and boil
Add distilled water

white emulsion if present

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12
Q

Composition of amino acid

A
  • central C atom
  • amino group NH2
  • carboxyl group COOH
  • side chain (R) varies in shape polarity + charge
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13
Q

Primary structure of protein

A

Sequence of amino acids joined by peptide bonds to form polypeptide chain

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14
Q

Secondary structure of protein

A

Folding of polypeptide into alpha helix or beta pleated sheet
- held in place by H bonds between NH and C=O of adjacent amino acids

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15
Q

Tertiary structure of protein

A

Further folding + formation of new bonds eg, H bonds, disulphide bridges, ionic bonds
R group determines these

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16
Q

Quaternary structure of protein

A

2 or more polypeptide chains are bound together - can contain prosthetic group

17
Q

Fibrous proteins

A

eg collagen

  • structural function
  • strong inter. forces
  • sheet like structure
  • insoluble
18
Q

Globular proteins

A

eg. enzymes, haemoglobin
- metabolic functions
- weak inter. forces
- 3D ball like structure
- soluble

19
Q

Induced fit hypothesis

A

Change in shape of enzymes active site induced by substrate -> fully complimentary after binding

20
Q

Activation energy

A

Minimum amount of energy needed by particles in a collision to cause a reaction

21
Q

Competitive inhibition

A

Inhibitor has complimentary shape to active site -> competes w/ substrate reducing no. of ES complexes formed

22
Q

Non-competitive inhibition

A

Inhibitor binds to enzyme changing the shape of the active site preventing any ES complexes from forming

23
Q

Factors affecting enzyme rates of reactions

A
  • temperature
  • pH
  • conc. of substrate
  • conc. of enzyme
  • inhibitors
24
Q

Difference between alpha and beta glucose

A
  • OH bottom right in alpha, top right in beta
  • alpha forms glycogen + starch
  • beta forms cellulose
25
Q

Test for non reducing sugar

A
  • heat solution w/ acid + neutralise
  • add benedict’s + heat
  • if blue -> orange/brown then non-reducing sugar present
26
Q

Ester bonds

A

Form in condensation reaction btw. glycerol + f.acid

27
Q

Peptide bonds

A

Form in condensation reaction btw. carboxyl + amino group

28
Q

Test for starch

A

Iodine

orange/brown to blue/black if present