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Biological Molecules Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

What are the 5 main biological molecules?

A

-carbohydrate
-lipids
-protein
-water
-nucleic acid

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2
Q

What are carbs, proteins and nucleic acids?

A

Macromolecules which are polymers

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3
Q

Type of reaction to turn. Polymer to a monomer.

A

Hydrolysis- water required to help break covalent bonds

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4
Q

Type of reaction needed to turn a monomer into a polymer.

A

Condensation- water is proved during covalent bond formation

Enzymes in cells beak down the bonds

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5
Q

3 main types of carbohydrate:

A

1) monosaccharides
2)disaccharides
3)polysaccharides

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6
Q

Type of monosaccharides:

A

Glucose- most abundant monosaccharides in nature and most common in food.

Other types: fructose, galactose, deoxyribose ribose

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7
Q

What are alpha and beta glucose?

A

They are isomers of glucose. Alpha glucose has hydrogen on the top right.

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8
Q

What are disaccharides ?

A

Simple sugars that consist of 2 monosaccharides bonded together with a glycosidic bond between carbon 1 and 4.

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9
Q

3 types of disaccharides

A

1) maltose (glucose + glucose)

2) sucrose (glucose + fructose)

3) lactose (glucose + galactose)

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10
Q

What is a glycosidic bond?

A

-chemical reaction forming the bond is a condensation reaction
- carbon 1 and 4 bonded
-chemical reaction that breaks the bond is hydrolysis due to need for water
-can be broken by boiling sugar in water + enzyme in cells lower activation energy so it happens in the body

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11
Q

What are polysaccharides?

A

Polymers of many monosaccharides joined via a glycosidic bond.

Large molecules that are insoluble so are suitable for storage e.g cellulose

When hydrolysed they break down in disaccharides and monosaccharides

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12
Q

An example of a polysaccharide

A

Starch found in starch grains in plants which is made of 200-100000 alpha glucose (condensation reaction) joined together

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13
Q

Explain the structure of amylose

A
  • alpha glucose monosaccharide (20-30%)
  • 1,4 glycosidic bond
    -forms a helix held together by hydrogen bonds which keeps it compact
  • insoluble in water so does not affect osmosis
  • helix can trap iodine to form a dark blue complex (starch test)
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14
Q

Explain the structure of amylopectin

A
  • alpha glucose monosaccharide (70%-80%)
  • 1,4 glycosidic bond with 1,6 glycosidic bond making side branches
  • soluble in hot and cold water
  • branching creates more terminal ends to chains allowing faster enzyme breakdown (hydrolysis)
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15
Q

Glycogen

A

-more highly branched than amylopectin
-important storage molecule
- branching creates more terminal ends to chains allowing faster enzyme breakdown
-stored as a compact glycogen granule
-alpha glucose monosaccharide
- 1,4 glycosidic bond and 1,6 glycosidic bond making side branch
-stored as glycogen as it needs to be accessed quickly branched for easy access.

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16
Q

Explain cellulose structure

A

-most abundant polysaccharide
- a structural polysaccharide only present in plants fungi and some bacteria
-beta glucose monomers
- 1,4 glycosidic bond
- adjacent beta glucose molecules rotate 180 degrees
-long straight chains
-parallel monomer chains form bigger fibres called myofibrils and macrofibrils.
-numerous hydrogen bonds hold ajacent chains together
-fibres created have a high tensile strength
- bonds can be digested using bacterial enzymes
-found in the cell walls of plants biofilm of some bacteria algae and fungi

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17
Q

What are the 2 types of lipids?

A

Triglyceride and phospholipid

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18
Q

Explain the structure of triglyceride

A

Consists of 3 fatty acids bonded to one glycerol molecule
Fatty acids = hydrocarbon with carboxylate acid group
Glycerol = hydroxyl group

Condensation reaction causes the bond to be formed this is between the -OH on the glycerol and -OH on the acid group. Bond formed is called an ester.

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19
Q

What are saturated and unsaturated fatty acids?

A

Saturated = all available bonds in the fatty acid chain have a hydrogen attached
Unsaturated = has a double bond between a carbon this makes the chain kink in that position this will cause the melting and boiling points to decrease because the fatty acid chains are spaced further apart. (Weaker intermolecular forces)

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20
Q

Explain the structure of a phospholipid

A

Consists of a glycerol molecule with 2 fatty acids and a phosphate group
- has a phosphate head and 2 fatty acid tails

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21
Q

5 main uses of lipids

A
  • energy source ATP ( oxidised to produce energy)
  • energy store
  • insulation (slow conductors of heat)
  • waterproofing (insoluble in water)
  • protection (delicate organs)
  • production of cholesterol and steroid hormones
22
Q

Phospholipids in water

A

-Insoluble but head is polar and hydrophilic
-Tails are hydrophobic and non-polar
This allows them to arrange in special structures in water
Liposomes micelles and bilayer sheets

23
Q

Triglycerides in water

A

-Water is a polar molecule so triglycerides are insoluble in water as they are non polar
- they can be dissolved in organic solvents,alcohol and acetone

24
Q

Polar Molecules

A
  • contain either oxygen, nitrogen or sulphur
    -have dipole charges
25
Q

Waters properties

A

-metabolite
- solvent
- high latency heat capacity
-cohesion
-specific heat capacity
-density and compressibility

26
Q

Water as a metabolite

A

-Used in many metabolic reactions like hydrolysis and condensation
-Byproduct of metabolic reactions

27
Q

Water as a solvent

A

Ionic and polar molecules such as biological molecules need to be dissolved into a polar solvent and water is good for this.

28
Q

Waters high latent heat capacity

A

-water has a high latent heat capacity as strength of hydrogen bonds. These bonds require lots of energy to be broken and vaporised.
-Water vaporisation can be used for calling down and uses a lot of heat and carried away sweating
-due to the high heat capacity the organism can call without using too much water or energy so they can survive

29
Q

Waters cohesion

A

-attraction between the same type of molecule
-Water has strong cohesion due to the hydrogen bonds
-Enables water to flow and transport for example in the xylem
-Produces surface tension so small organisms walk on water

30
Q

Specific heat capacity of water

A

-hi so a lot of energy is needed to change the temperature so water has a constant temperature
-Makes the ocean a thermally stable habitat

31
Q

Waters density and incompressibility

A

-max density is 4° when water turns to ice and becomes less dense which floats creating insulation. This is due to molecules being further apart.(ocean habitat)
-Incompressible due to strong intermolecular bonds between molecules

32
Q

What is an amino acid?

A

-made of an amine group and carboxylic group
-only r group varies

33
Q

What is a peptide bond?

A

-a bond between 2 amino acids to form a polypeptide chain
-condensation reaction that takes place inside ribosomes
-catalysed via specific enzymes and hydrolysed via protease enzymes

34
Q

What is a protein?

A

A folded polypeptide chain of which is able to perform a specific function

35
Q

What is the primary structure of a protein?

A

-specific order of amino acids which determines final shape of protein
-determined via dna

36
Q

What is the secondary structure of a protein?

A

-hydrogen bonds form between positive -NH group and negative -CO
-causes chain to twist and fold into specific shapes
-alpha helix or beta plaited sheet

37
Q

What is the tertiary structure of a protein?

A

-overall 3D shape of the protein which is critical to its function
-bonds such as ionic, dulsulphide and hydrogen bonds as well as hydrophobic bonds cause this to happen

38
Q

What is the quaternary structure of a protein?

A

-proteins with more the one polypeptide chains
-called subunits the structure shows how these are arranged and shows the position of prosthetics
-prosthetics are non protein structures in a protein helping it to carry out the role

39
Q

What is a protein called if it contains prosthetics?

A

Conjugated protein

40
Q

What is the lock and key model of enzymes?

A

The shape of an active site is complementary to the substrate

41
Q

What are enzymes?

A

-Biological catalysts that speed up the rate of the reaction
-made of protein
-lower activation energy to start a reaction
-biological molecules are held via covalent bonds so usually need enzymes to break them

42
Q

What is the induced fit model of enzymes?

A

-active site is not complementary to substrate that it acts on
-charged amino acids in active site hold the substrate in place
-on binding the active site changes shape the change in shape either bends bonds in substrate (catabolic reaction) or forces substrate closer together (anabolic reaction)
-products formed are a different shape to substrate so no longer fit active site and move away from

43
Q

Temperatures effect on enzyme controlled reactions

A

higher temperature:
-faster rate of collisions with active site and substrate
-with more energy
-so faster ESC formation

Enzyme will denature and active site changes as bonds break causing a change in the tertiary structure. Although primary structure is not affected denaturation is not reversible.

44
Q

pH effect on enzyme controlled reactions

A

The tertiary structure of the enzyme is maintained by hydrogen and ionic bonds therefore pH will affect the active site of an enzyme. Many active sites involved in catalysis are charged of which is changed by the pH as the H+ ions are attracted towards the negatively charged residue

All enzymes have optimum pH this is the H+ concentration that gives their tertiary structure best overall shape to bind to substrate. Usually around 7 the range of which the enzyme will work is narrow.

45
Q

Concentration effect on enzymes

A

As concentration increases the reaction rate will increase due to increased collisions between active site and substrate so more esc is formed

46
Q

Enzyme substrate effect on concentration

A

The greater concentration of substrate means a higher rate due to increased collisions and Avaliable active sites however the active sites will become a limiting factor and the rate will plateau.

47
Q

Enzyme concentration effect on enzymes

A

The increase in enzyme concentration will cause an increase in the rate of reaction up to a specific point as greater avaliable active sites for substrate however the rate plagues as not all active sites are saturated as substrate becomes a limiting factor

48
Q

Enzyme inhibitors

A

Reduce the rate of enzymes via acting on an enzyme in a specific way.

49
Q

Competitive inhibition

A

Inhibitors have:
-similar shape to substrate
-shape complementary to active site
-occupy active site to form enzyme inhibitors complex so substrate is prevented from occupying the active site so there are less ESC so rate slows

Need greater amounts of substrate to reach higher rates in the presence of the inhibitor

50
Q

Non Competitive Inhibition

A

-do not compete with substrate for active site as they have a separate binding point to enzyme called allosteric site.
-when binded it distorts shape of active site
-with enough inhibitors reaction will stop

The greater amount of inhibitors the slower the rate of reaction and the faster the rate will plateau due to quickly running out of active sites

51
Q

Permanent/non permanent inhibitors

A

Permanent - enzyme is denatured
Non -permanent - removal of inhibitor leaves enzyme ready for catalysis
General rule - competitive = non-permanent non-competitive = permanent

Biology (5 decks)

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