Section 1: Biological Molecules Flashcards

1
Q

What is a monomer?

A
  • Small, single molecule which can be joined together to form a polymer
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

What is a polymer?

A
  • Large molecule made of monomers joined together
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

What is a condensation reaction?

A
  • Joins 2 molecules together
  • Eliminates a water molecule
  • Forms a chemical bond e.g. glycosidic bond
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

What is a hydrolysis reaction?

A
  • Separates 2 molecules
  • Breaks a chemical bond using water
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

Names some monomers and their polymers.

A
  • Nucleotide - Polynucleotide
  • Monosaccharide - Polysaccharide
  • Amino acid - Polypeptide (protein)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

What is a monosaccharide?

A
  • Monomers from which larger carbohydrates are made
  • E.g. glucose, fructose and galactose
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

How do you draw an Alpha glucose?

A
  • The OH group is below the plane of the ring
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

How do you draw a Beta glucose?

A
  • The OH group is above the plane of the ring
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

How are disaccharides formed and what molecules are required to make each?

A
  • Formed by the condensation of 2 monosaccharides
  • Glucose + Glucose = Maltose
  • Glucose + Fructose = Sucrose
  • Glucose + Galactose = Lactose
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

What is the structure and function of glycogen?

A
  • Energy store in animal cells
  • Polysaccharide of a-glucose with C1-C4 and C1-C6 glycosidic bonds so it is branched
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

What is the structure of glycogen suited to its function?

A
  • Branched; rapidly hydrolysed to release glucose for respiration to provide energy
  • Large polysaccharide molecule, can’t leave
  • Insoluble in water, water potential of cell not affected
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

What is the structure and function of starch?

A
  • Energy store in cells
  • Polysaccharide of a-glucose, unbranched or branched
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

What is the structure related to its function?

A
  • Helical, compact for storage in cells
  • Large polysaccharide, can’t leave cell
  • Insoluble in water, WP not affected
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

What is the function of cellulose?

A
  • Provides strength and structural support to plant cell walls
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

What is the structure related to its function of cellulose?

A
  • Every other beta glucose molecule is inverted in a long straight unbranched chain
  • Many hydrogen bonds link parallel strands to form microfibrils
  • H bonds are strong in high numbers
  • Provides strength and structural support to plant cells
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

What are examples of reducing and non-reducing sugars?

A
  • Reducing sugar : Monosaccharides, some disaccharides (maltose/ lactose)
  • Some disaccharides - sucrose
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

What is the Benedict’s test for reducing sugars?

A
  • Add Benedicts reagent to sample and heat in a boiling water bath
  • Positive = green/yellow/orange/red percipitate
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

What is the Benedict’s test for non-reducing sugars?

A
  • Add a few drops of dilute hydrochloric acid
  • Heat in a boiling water bath
  • Neutralise with sodium hydrogen carbonate
  • Add Benedict’s reagent and heat again
  • Non-reducing sugar present = green/yellow/ orange/ red percipitate
19
Q

How do you determine glucose concentration?

A
  • Produce a dilution series of glucose solutions of known concentrations
  • Perform a Benedict’s test on each sample
  • Using a colorimeter, measure the absorbance of each sample and plot a calibration curve
  • Repeat with unknown sample (find absorbance) and use graph to determine glucose concentration
20
Q

What is the Iodine test for starch?

A
  • Add iodine to solution and shake/stir
  • Blue-black colour = starch present
21
Q

What are the 2 groups of lipids?

A
  • Triglycerides and Phospholipids
22
Q

How are triglycerides formed?

A
  • Formed by the condensation of 1 molecule of glycerol and 3 fatty acids. Forms ester bonds
22
Q

How are triglycerides formed?

A
  • Formed by the condensation of 1 molecule of glycerol and 3 fatty acids. Forms ester bonds
23
Q

What are the properties of triglycerides related to its function?

A
  • High ratio of C-H bonds to C atoms in hydrocarbon tail so release more energy than the same mass of carbohydrates
  • Insoluble in water so no effect on WP
24
Q

How are Phospholipids formed?

A
  • One of the fatty acids of a triglyceride is substituted by a phosphate- containing group
25
Q

What are the properties of phospholipids related to its function?

A
  • Phospholipids form bilayers in cell membranes allowing diffusion of non-polar
  • Phosphate heads are polar/ hydrophilic so are attracted to water orient to aqueous environment
  • Fatty acid tails are non-polar/ hydrophobic so are repelled by water - orient to interior of membrane
26
Q

What is the emulsion test for lipids?

A
  • Add ethanol and shake
  • Add water
  • Positive: milky/ white emulsion
27
Q

What is the general structure of an amino acid

28
Q

What is the primary structure of a protein?

A
  • Sequence of amino acids in a polypeptide chain
29
Q

What is the secondary structure of a protein?

A
  • Hydrogen bonding between amino acids between carbonyl O and amino H of another
  • Causes polypeptide chain to coil into alpha helix or fold into a beta pleated sheet
30
Q

What is the tertiary structure of a protein?

A
  • Overall 3D structure of a polypeptide held together held by interactions between amino acid side chains
  • Ionic bonds/ disulfide chains/ hydrogen bonds
31
Q

What is the Quaternary structure of a protein?

A
  • Some proteins are made of 2+ polypeptide chains
  • Held together by more hydrogen, ionic and disulfide chain bonds
32
Q

What is the test for proteins?

A
  • Add biuret solution: sodium hydroxide + Copper sulfate
  • Protein present = purple/ lilac colour
  • Detects peptide bonds
33
Q

What do enzymes do?

A
  • Lowers the activation energy of the reaction it catalyses - speed up the rate of reaction
  • Enzymes are biological catalysts
34
Q

What is the lock and key model?

A
  • Active site is a fixed shape/ doesn’t change shape
  • It is complementary to 1 substrate
  • After a successful collision, an enzyme-substrate complex forms leading to a reaction
35
Q

What is the Induced Fit Model?

A
  • Before reaction, enzyme active site not completely complementary to substrate
  • Active site shape changes as substrate binds and enzyme-substrate complex forms
  • This stresses/ distorts bonds in substrate leading to a reaction
36
Q

What are the Factors that affect the rate of enzyme-controlled reaction?

A
  • Enzyme Concentration
  • Substrate Concentration
  • Temperature
  • pH
37
Q

How does increasing enzyme concentration affect the rate and when does it plateau?

A
  • Increases the rate when enzyme conc is the LF
  • More enzymes - more available active sites
  • More successful E-S collisions and E-S complexes
  • At a certain point Substrate conc = LF
38
Q

How does increasing the substrate concentration affect the rate of a reaction and when does this plateau?

A
  • Rate of reaction increases when substrate concentration is the LF
  • More successful collisions and E-S complexes
  • Enzyme conc = LF
39
Q

How does increasing temperature affect the rate of reaction?

A
  • Rate of reaction increases
    • Increase in Kinetic Energy
    • More successful E-S complexes
40
Q

What happens when increasing temperature above optimum?

A
  • Rate of reaction falls
  • Enzymes denature, tertiary structure and active site changes shape
  • Fewer E-S collisions and E-S complexes
41
Q

What happens to the rate of reaction with pH above and below the optimum?

A
  • Enzymes denature, tertiary structure and active site changes shape
  • Complementary substrate can no longer binds
  • Fewer E-S complexes
42
Q

How do competitive inhibitors decrease the rate of reaction?

A
  • Similar shape to substrate
  • Competes for/ blocks / binds to active site so substrates can’t
  • Fewer E-S complexes
  • Increasing substrate conc reduces the effect of inhibitors
43
Q

How do non-competitive inhibitors decrease the rate of reaction?

A
  • Binds to site away from the active site
  • Enzyme tertiary structure/ active site changes shape so substrate can’t bind
  • Fewer E-S complexes
  • Increasing substrate concentration has no effect