B1. Biological Molecules (DONE) Flashcards

You may prefer our related Brainscape-certified flashcards:
1
Q

What is covalent bonding?

A

Electrons in valence shell are shared

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

What is ionic bonding?

A

Ions with opposite charges attract each other, weaker than covalent bonds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

What is hydrogen bonding?

A

Attractive force between partially positive charged hydrogen attached to electronegative atom of one molecule and an electronegative atom of a different molecule

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

What is polymerisation?

A

Monomers joining together to make a long molecule, polymer

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

What is a condensation reaction?

A

Joins monomers by chemical bond and involves the elimination of a water molecule

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

What is a hydrolysis reaction?

A

Break chemical bond between molecules with the use of water

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

What is the definition of metabolism?

A

Sum of all chemical processes in an organism

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

What are organic molecules?

A

Carbon containing molecules

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

What are the monomers of a carbohydrate?

A

Saccharide (sugar); Monosaccharide (single unit); Disaccharide (2 units); Polysaccharide (more than 2 units)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

What is the test for reducing sugars?

A

Add benedict’s solution (Copper(II) Sulfate and Sodium hydroxide), heat in water bath; Reducing sugar donates electron to benedict’s solution; Precipitate of Copper(I) Oxide formed; Blue to brick red

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

What is the test for non-reducing sugars?

A

Boil sugar w/ dilute HCl in water bath; Neutralise solution with Sodium Hydrogen Carbonate; Red litmus paper to test pH, solution needs to be slightly alkaline; Carry out Benedict’s test

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

What are the equations for the formation of major disaccharides?

A

Glucose + Glucose => Maltose
Glucose + Fructose => Sucrose
Glucose + Galactose => Lactose

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

How do monosaccharides bond and break bonds?

A

Condensation reaction, forming glycosidic bond; Bonds broken by hydrolysis reactions

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

What is the test for starch?

A

Add drops of Potassium Iodide; Starch changes Iodine in solution from yellow to blue black

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

What makes Glycogen and Starch good storage molecules?

A

Compact; Insoluble, no osmotic effect that would change a cells water potential

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

What is Glycogen and what are its properties?

A

Animal and fungi storage polysaccharide; Highly branched not coiled, easily hydrolysed to glucose; High concentration in live and muscle cells;

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

What are the polysaccharides that make up starch?

A

Amylose 10% - 30%; Amylopectin 70% - 90%

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

What are the properties of amylose?

A

Unbranched helix chain shape; 1,4 glycosidic bonds; Helical shape allows it to be more compact, more resistant to digestion

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

What are the properties of amylopectin?

A

1,4 glycosidic bonds; 1,6 glycosidic bonds between glucose molecules creating branched molecule; Branched chains, easy hydrolysis for cellular respiration

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

What is starch?

A

Storage polysaccharide for plants; stored as granules in plastids; Longer to digest than glucose due to many monomers

21
Q

What is cellulose and what are its properties?

A

Consists of beta glucose; Structural carbohydrate; Neighbour molecules, 180 degree rotated due to H, OH group on beta glucose; Straight unbranched chains; Cross linkages between adjacent chains; Keeps cell turgid by exerting inward force; Microfibrils; Fibres

22
Q

What are the roles of lipids?

A

Energy source, 2x more than carbohydrates; Waterproofing, hydrophobic; Insulating, Slow conductors; Protection, stored around delicate organs; Non polar

23
Q

What do fats and oils consist of?

A

Fats, saturated fatty acids; Oils, unsaturated fatty acids

24
Q

What is the structure of glycerol?

A

C3H8O3; carbon molecule w/ 3 alcohol groups (OH)

25
Q

What is the structure of fatty acids?

A

Long molecule; Non polar hydrocarbon chain (R group); R-COOH polar carboxyl group

26
Q

How are triglycerides formed?

A

1 glycerol molecule forms 3 ester bonds with 3 fatty acids in a condensation reaction (3H2O); Fatty acid carboxyl group w/ glycerol alcohol group

27
Q

What is the difference between a saturated and unsaturated fatty acid?

A

Saturated fatty acid, no double bonds; Unsaturated, double bonds; Monounsaturated fatty acid, 1 =; Polyunsaturated fatty acid, more than 1 =

28
Q

What is the structure of a phospholipid?

A

Hydrophilic head, attracted to H2O; Hydrophobic tail, oirients away from H2O but mixes w/ fat

29
Q

How do you test for lipids?

A

Emulsion test; Add ethanol; Shake thoroughly, dissolve lipids; Add water, shake gently; Cloudy white emulsion

30
Q

What are the monomers of a phospholipid?

A

2 fatty acid molecules and 1 phosphate molecule bonded to a glycerol molecule

31
Q

What is the structure of an amino acid?

A

Amino group left (NH2); Carbon; Carboxylic group right (COOH); H above; R group side chain bellow (20 unique types)

32
Q

How do amino acids bond?

A

Peptide bonds between C, N; 2 amino acids, dipeptide; 2+, polypeptide; Condensation reaction between carboxyl group and H;

33
Q

What is the primary structure of proteins?

A

Sequence of amino acids bonded by covalent peptide bonds; DNA, responsible for primary structure, instructs order of amino acids

34
Q

What is the secondary structure of proteins?

A

Hydrogen bonds between (amino group) N - O (carboxyl group) causes: α-helix, H bond between every 4th peptide bond; β-pleated sheet, folds so 2 parts of polypeptide chain are parallel, H bonding between parallel peptide bonds; High temperature and pH changes can break H bonds

35
Q

What level of structure do most fibrous proteins have?

A

Secondary structure eg. collagen, keratin

36
Q

What is the tertiary structure of proteins?

A

Helices folded to form unique 3D structure; Conformational changes of secondary structure lead to additional bonds forming between R groups; Hydrogen, Disulphide, Ionic; Common in globular proteins

37
Q

What is the quaternary structure of proteins?

A

Proteins that have more than 1 polypeptide chain working together as functional macromolecule; Each polypeptide chain is referred to as a subunit

38
Q

What are enzymes?

A

Globular proteins that act as a biological catalyst; Speed up rate of reaction without being used up for altering itself

39
Q

What is the test for proteins?

A

Treat liquid solution w/ sodium hydroxide, make alkali; Add few drops of copper(II) sulfate; (biuret solution, alkali + copper(II) sulfate) ; Blue to lilac

40
Q

Describe the structure of enzymes.

A

Globular protein, specific 3D shape; Substrate binds to active site forming enzyme substrate complex; Active site has specific shape; Extreme heat or pH change can denature active site; Shape of active site is determined by tertiary structure

41
Q

How does the lock and key model function?

A

Substrate fits exactly into active site, enzyme substrate complex; Reaction takes place, enzyme product complex formed; Product released

42
Q

How does the induced fit model function?

A

Substrate does not fit perfectly into active site; Active site undergoes conformational change; Enzyme substrate complex formed; Reaction takes place, enzyme product complex; Products released

43
Q

How can you measure an enzyme catalysed reaction

A

Formation of products to disappearance of substrates; Plot graph, find gradient y/x

44
Q

What are the effects of increasing temperature and changing pH on enzyme reaction?

A

Increased kinetic energy, more collisions, bonds in enzymes break; 60c enzyme denatures; pH change alters amino acid charges, denaturing active site; pH change breaks bonds in tertiary structure, denaturing active site

45
Q

What is standard deviation used to measure?

A

Measures spread of all data in relation to the mean

46
Q

What are enzyme inhibitors?

A

Substances that directly or indirectly interfere with the active site, reducing activity

47
Q

What are competitive inhibitors?

A

Enzyme inhibitor; Similar molecular shape to substrate; Compete with substrate for active site; Non permanent; Lowers rate of complex

48
Q

What are non competitive inhibitors?

A

Enzyme inhibitor; Binds to enzyme’s allosteric site; Alters shape of active site; Prevents enzyme substrate complex; Permanent; Lowers rate of complex