2. Biological Molecules Flashcards

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1
Q

Describe the Benedict’s test for reducing sugars

A

-add equal volume of Benedict reagent to the sample to be tested.
-heat the mixture in a water bath at 100 degrees for 5 minutes
Positive result- blue to a green to yellow to orange to brick red

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2
Q

Describe the iodine test for starch

A

-add a few drops of iodine to the sample
-if starch is present, iodide ions in the solution interact with the Centre of starch molecules, producing with a distinctive blue-black colour

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3
Q

Describe the Benedict test for non-reducing sugars

A
  1. hydrolyse non reducing sugars into their monomers by adding an equal volume of HCl
  2. Heat in a boiling water bath for 5min
  3. Neutralize the mixture using sodium hydrogen carbonate solution
  4. Proceed with the Benedict’s test as usual.
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4
Q

Describe the emulsion test for lipids.

A

-add ethanol to the sample to be tested, shake to mix then add the mixture to a test tube of water
-if lipids are present, a milky emulsion will form
-if no lipid is present, the solution remains clear.

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5
Q

Describe the outer test for proteins.

A

-a liquid solution of sample is treated with sodium or potassium hydroxide to make the solution alkaline.
-a few drops of copper(II) sulfate is added to the sample
-if protein is present, a color change from blue to lilac/purple will be observed

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6
Q

Describe a semi-quantitative Benedict’s test on a reducing sugar solution.

A

-can be carried out by setting up standard solutions with known concentrations of reducing sugar
-using serial dilution.
-each solution is then treated in the same way; add the same volume of Benedict’s solution to each sample and heat in a water bath that has been boiled.
-any color change observed for each solution of a known concentration of reducing sugars is then compared to the stock solution colors.

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7
Q

Define the term monomer

A

A single subunit that is used to build large polymers

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8
Q

Define the term polymer

A

A large molecule comprised of repeating subunits

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9
Q

Macromolecule

A

A large biological molecule
Eg: polysaccharides
Proteins (polypeptides)
Nuclei acids (polynucleotides)

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10
Q

What is the difference between alpha and beta glucose?

A

The OH group on carbon 1 for alpha glucose is below the ring, while that for the beta glucose is above the ring.

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11
Q

Define a monosaccharide

A

A single sugar monomer, all of which are reducing sugars

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12
Q

What is a disaccharide

A

A sugar formed from two monosaccharides joined by a glycosidic bond in a condensation reaction

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13
Q

What is a polysaccharide

A

A polymer formed by many monosaccharides joined by a glycosidic bond in a condensation reaction

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14
Q

Why are triglycerides energy reserves ?

A

Because they store more energy per gram due to their hydrocarbon chains.

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15
Q

What is a condensation reaction?

A

A chemical reaction involving the joining together of two molecules by removal of a water molecule

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16
Q

What is a hydrolysis reaction?

A

A chemical reaction in which a chemical bond is broken by the addition of a water molecule; commonly used to break down complex molecules into simpler molecules.

17
Q

Equation for sucrose

A

Glucose+fructose

18
Q

Equation for maltose

A

Glucose+ glucose

19
Q

Equation for lactose

A

Glucose+galactose

20
Q

Functions of triglycerides

A
  1. They make excellent energy stored because they are richer in carbon-hydrogen bonds than carbohydrates
  2. They act as an insulator against loss of heat just below the skin
  3. Metabolic source of water- when triglycerides are oxidized in respiration, they are converted to carbon dioxide and water.
21
Q

What is the primary structure in a protein?

A

The sequence of amino acids in a polypeptide or protein.

22
Q

What is a secondary structure in proteins?

A

The structure of a protein molecule resulting from the regular coiling or folding of the chain of amino acids (an ą-helix or B-pleated sheet)

23
Q

What is the tertiary structure of a protein?

A

The compact structure of a protein resulting from the three-dimensional coiling of the chain of amino acids.

24
Q

What is the quaternary structure of a protein?

A

The three-dimensional arrangement of two or more polypeptides, or of a polypeptide and a non-protein component such as haem, in a protein molecule.

25
Q

What is a globular protein?

A

A protein whose molecules are folded into a spherical shape, it is often water-soluble.

26
Q

Why do globular proteins usually curl up?

A

So that their non-polar hydrophobic R groups point into the centre of the molecule, away from the watery surroundings.

27
Q

What is a fibrous protein?

A

A protein whose molecules have a relatively long, thin structure that is generally insoluble and whose function is usually structural.

28
Q

What is the latent heat of vaporization?

A

A measure of the heat energy needed to vaporize a liquid changing it from a liquid to a gas.

29
Q

Disulphide bonds

A

Strong covalent bonds that form between two cysteine R groups
Strongest bonds in a protein molecule

30
Q

Ionic bonds

A

Form between positively charged and negatively charged R groups
Stronger than hydrogen bonds

31
Q

Hydrogen bonds

A

Form between strongly polar R groups

32
Q

Hydrophobic interactions

A

Form between the non-polar (hydrophobic) R groups