Chapter 1- Biological Molecules Flashcards

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1
Q

Monomer

A

Smaller units used to make larger molecules

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2
Q

Polymer

A

Molecules made from monomers joined together (complex + large)

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3
Q

Condensation reaction

A

Joins 2 monosaccharides by forming a glycosidic bond and removing water

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4
Q

Hydrolysis reaction

A

Water added to disaccharide to break the bond and release the monosaccharides.

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5
Q

What are the 3 monosaccharides?

A

Glucose, galactose, fructose

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6
Q

What are the two isomers of glucose?

A

Alpha and beta

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7
Q

How are disaccharides formed?

A

In a condensation reaction

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8
Q

Glucose + glucose ->

A

Maltose

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9
Q

Glucose + fructose ->

A

Sucrose

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10
Q

Glucose + galactose ->

A

Lactose

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11
Q

Test for reducing sugars

A
  1. Add equal volume of sample + Benedict’s to test tube
  2. Heat in water bath
  3. Turns red/orange
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12
Q

Test for non-reducing sugars

A

1 . Negative Benedict’s test
2. + dilute HCl + gently boil =in water bath
3. Add sodium hydrogen carbonate to neutralise
4. Repeat Benedict’s
5. Colour change if positive

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13
Q

Test for starch

A
  1. Add 2 drops iodine solution + shake
  2. Colour change to blue-black if present
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14
Q

Monomer in starch

A

Alpha glucose

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15
Q

Function of starch

A

Energy storage

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16
Q

How does the structure of starch relate to its function?

A

-Insoluble = X affect water potential
-Large = X diffuse out
-Compact = a lot in small space
-Hydrolysed into alpha glucose = easily transported for respiration
-Branched = has many ends = enzymes act simultaneously = rapid energy release

17
Q

Monomer in glycogen

A

Alpha glucose

18
Q

Function of glycogen and in what organisms?

A

Carbohydrate store in animals + bacteria

19
Q

How does the structure of glycogen relate to its function?

A

-Insoluble = X affect osmosis
-Compact = lot in small space
-Highly branched = > ends to act on = rapid glucose release for respiration

20
Q

Monomer in cellulose

A

Beta glucose (every other one is inverted)

21
Q

Structure of cellulose

A

Straight, unbranched, parallel chains = H bonds for cross linkages for strength

22
Q

How are the cellulose chains grouped?

A

In microfibrils + then fibres

23
Q

Function of cellulose

A

Plant cell walls -> adds rigidity by exerting inward pressure stopping water influx and making it turgid

24
Q

Roles of lipids

A

Cell membranes, energy, waterproofing, insulation, organ protection

24
Q

What elements do lipids contain?

A

C,H,O

25
Q

Test for lipids

A
  1. Add ethanol + shake
  2. Add water + shake
    • result = cloudy
26
Q

What do triglycerides contain?

A

3 fatty acids + a glycerol
Ester bond attaches FAs to glycerol

27
Q

Difference between saturated and unsaturated Fatty acids

A

Saturated has no C=C
Unsaturated has 1 or > C=C

28
Q

How does structure of triglycerides relate to their function?

A

-High ration of C-H bonds to C atoms = energy store
-Low mass:energy = good store (> energy in small V)
Large, non-polar = insoluble = X affect water potential
-High H:O = releases water when oxidised (water source)

29
Q

Structure of phospholipids

A

2 fatty acids, glycerol + phosphate group

30
Q

What are the two parts of a phospholipid?

A

Hydrophilic head + hydrophobic tail

31
Q

How do the 2 parts of a phospholipid work together?

A

Form a bilayer within cell-surface membranes = acts as a hydrophobic barrier + contributes to flexibility + transfer of lipid-soluble substances

32
Q

Test for proteins

A
  1. Add Biuret reagent to sample
  2. Positive result = turns purple
33
Q

Structure of an amino acid

A

Central carbon attached to 4 chemical groups = amine, carboxyl, hydrogen atom + a variant R group

34
Q

Explain the formation of a peptide bond

A

-Condensation reaction - water made up of H of amine group + OH of carboxyl group forming a dipeptide
-Bond broken through hydrolysis reaction

35
Q

Primary structure of a protein

A

Specific sequence of amino acids (joined by polymerisation) -> determines shape + therefore function

36
Q

Secondary structure of a protein

A

Polypeptide folds + H bonds form within

37
Q

Tertiary structure of a protein

A

-Folding into a 3D structure
-Bonding between amino acids determined by primary structure
-Makes each protein distinctive
Bonds:
-Disulfide bridges
-Ionic bonds - between carboxyl + amine groups -> easily broken by pH changes
-H bonds - can be easily broken

38
Q

Quaternary structure of a protein

A

-Complex + has multiple polypeptide chains
E.g. haemoglobin
-Can have prosthetic (non-protein group) attached