Biological Molecules Flashcards

1
Q

What are monomers?

A

Monomers are small units which are the components of larger molecules

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2
Q

Give examples of monomers

A
  • Amino acids
  • Glucose
  • Nucleotides
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3
Q

How are polymers formed?

A

From many monomers joining together via a condensation reaction

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4
Q

What are carbohydrates?

A

Molecules consisting of only carbon, hydrogen and oxygen

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5
Q

Common monosaccharides

A
  • Glucose
  • Fructose
  • Galactose
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6
Q

Common disaccharides and how they are formed

A
  • Maltose is a disaccharide formed by condensation of two glucose molecules.
  • Sucrose is a disaccharide formed by condensation of glucose & fructose.
  • Lactose is a disaccharide formed by condensation of glucose & galactose.
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7
Q

Name the polysaccharides and how they are formed

A
  • Glycogen and starch which are both formed by the condensation of alpha glucose.
  • Cellulose formed by the condensation of beta glucose
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8
Q

Why is Glycogen a good storage molecule?

A
  • Very branched so energy can be released quickly
  • Large but compact molecule maximising the amount of energy that can be stored
  • It is insoluble so does not affect the water potential of the cell
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9
Q

How is glycogen formed

A

Many glucose molecules joined up by 1,4 and 1,6 glycosidic bonds

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10
Q

Why is starch a good storage molecule?

A
  • Amylose is an unbranched chain of glucose molecules joined by 1,4 glycosidic bonds. So it is coiled and very compact
  • Amylopectin is branched and the glucose molecules are joined up by 1,4 and 1,6 glycosidic bonds. The side branches allow enzymes to work simultaneously to release energy
  • Starch is insoluble so will not affect water potential
  • Compact so a lot of energy can be stored
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11
Q

How is cellulose formed?

A

Via long, unbranched chains of beta glucose

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12
Q

What do cellulose chains form?

A

They form microfibrils that are parallel cellulose chains joined up by hydrogen bonds

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13
Q

Why is cellulose important?

A

It provides structural support for cells and maximises surface area for photosynthesis as it exerts inward pressure that stops the influx of water, keeping the cell rigid and turgid

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14
Q

How to test for a reducing sugar

A
  • Add Benedict’s reagent to a sample and bring the solution to a boil
  • If positive a precipitate should form, from blue to green/ yellow/ orange/ brick-red
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15
Q

How to test for a non reducing sugar

A
  • Carry out the test for a reducing sugar
  • Take a new sample
  • Add dilute hydrochloric acid and sodium hydrogencarbonate and place in a boiling water bath
  • Add Benedict’s reagent
  • If positive a coloured precipitate will form
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16
Q

What is the test for starch?

A
  • Iodine dissolved in potassium iodide

- If positive solution will turn from orange/brown to blue/black

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17
Q

What is the monomer for proteins

A

Amino acids

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18
Q

What is the structure of an amino acid?

A

An amino group and a carboxyl group

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19
Q

How are dipeptides formed?

A

Formed via a condensation reaction between 2 amino acids joined by a peptide bond and releasing a molecule of water.

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20
Q

What is the primary structure of an protein?

A
  • Order and number of amino acids in a protein
  • The initial sequence of amino acids which will therefore
    determine the proteins function in the end.
21
Q

What is the secondary structure of a protein?

A
  • Weak hydrogen bonds form between the amino acids in the chain to either coil into an alpha helix or fold into a beta pleated sheet
22
Q

What is the tertiary structure of a protein?

A
  • The further coiling or folding of the amino acid chain
  • More hydrogen bonds (easily broken)
  • Ionic bonds between the carboxyl and amino group not involved in the peptide bonds (can break due to changes in pH)
  • Disulfide bridges in cysteine (strong, not easily broken)
23
Q

What is the quaternary structure of a protein?

A
  • Made of several polypeptide chains put together

- The final 3D structure eg, haemoglobin

24
Q

Example of globular proteins

A

Enzymes - they are compact

25
Q

Example of fibrous proteins

A

Keratin are long so can fibres

26
Q

Describe the test for proteins

A
  • Add sodium hydroxide to the sample
  • Then add copper sulfate
  • If positive solution will turn from blue to purple
27
Q

What are enzymes?

A

Proteins that increase the rate of reactions by lowering the activation energy by providing an alternative pathway without being used up

28
Q

Factors that affect the rate of enzyme controlled reactions

A
  • Temperature
  • pH
  • Enzyme concentration
  • Substrate concentration
  • Concentration of competitive inhibitors
  • Concentration of non competitive inhibitors
29
Q

How does temperature affect the rate of enzyme controlled reactions?

A
  • Rate increases until it reaches the optimum temp
  • Above optimum, the enzymes become denatured as the hydrogen bonds in the tertiary structure break, so rate of reaction decreases
30
Q

How does pH affect the rate of enzyme controlled reactions?

A
  • It changes the ionic and hydrogen bonds in the tertiary structure changing the shape of the active site
31
Q

How does enzyme concentration affect the rate of enzyme controlled reactions?

A
  • Rate increases as the enzyme concentration increases as there are more active sites to form enzyme-substrate complexes
  • If will level off when substrate becomes the limiting factor
32
Q

How does substrate concentration affect the rate of enzyme controlled reactions?

A
  • As substrate concentration increases, rate of reaction increases as more enzyme-substrate complexes are formed
  • Eventually it will level off as enzyme concentration becomes the limiting factor
33
Q

How does the concentration of competitive inhibitors affect the rate of enzyme controlled reactions?

A
  • As the concentration of competitive inhibitors increases, the rate decreases
  • As substrates cannot bind
34
Q

How does the concentration of non competitive inhibitors affect the rate of enzyme controlled reactions?

A
  • As concentration on noncompetitive reversible inhibitors increases, rate of reaction decreases
  • As it changes the shape of the active site
35
Q

What does a DNA nucleotide contain?

A
  • Deoxyribose sugar
  • Phosphate group
  • Nitrogenous bases; adenine, cytosine, guanine or thymine
36
Q

What does a RNA nucleotide contain?

A
  • Ribose sugar
  • Phosphate group
  • Nitrogenous bases; adenine, cytosine, guanine or uracil.
37
Q

What bond is found between nucleotides?

A

Phosphodiester bonds

38
Q

Where is the phosphodiester bond formed?

A

Between the deoxyribose of one nucleotide and the phosphate group of another

39
Q

The steps of semi-conservative replication

A
  • DNA helicase breaks the hydrogen bonds between the complementary base pairs to leave to strands
  • One strand acts as a template for free DNA nucloetides to line up against
  • The nucleotides are joined together by phosphodiester bonds and hydrogen bonds form between the complementary base pairs
40
Q

How is energy released from ATP?

A

Through hydrolysis of ATP forming ADP and an inorganic phosphate. Catalysed by ATP hydrolase

41
Q

Where is the energy released from in ATP?

A

Stored as chemical energy in the phosphate bonds, it is released through the breaking of the bond catalysed by ATP hydrolase.

42
Q

Why is ATP a good source of energy?

A
  • It can be broken down easily due to the phosphate bonds being unstable, so quick energy release
  • It is a small, soluble molecule so it can be transported around the cell
  • It stores and releases small, manageable amounts of energy, so no energy is lost through heat
  • It can be remade quickly
  • Makes other molecules more reactive due to its phosphate groups
  • Provides an immediate supply of energy
43
Q

What can the inorganic phosphate be used for?

A

To phosphorylate other compounds making them more reactive

44
Q

How is ATP produced?

A

Through the condensation of ADP and inorganic phosphate catalysed by ATP synthase forming ATP during photosynthesis and respiration.

45
Q

Properties of ATP

A
  • ATP is an immediate source of energy as it can be broken down in a single step to release a manageable quantity of energy.
  • ATP is not stored in large quantities as it can easily be reformed from ADP in seconds.
  • ATP is used in a variety of different ways, such as metabolic processes, movement, active transport, secretion and activation of molecules.
46
Q

Function of hydrogen ions

A

Determines the pH of substances such as blood – the higher the concentration of hydrogen ions the lower the pH

47
Q

Function of iron ions

A

Component of haemoglobin which is an oxygen carrying molecule in red blood cells

48
Q

Function of sodium ions

A

Involved in co-transport of glucose and amino acids

49
Q

Function of phosphate ions

A
  • Component of DNA, RNA and ATP

- Allow nucleotides to join up