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Biology AS > Biological Molecules > Flashcards

Biological Molecules Flashcards

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1
Q

Define monomer :

A

smallest units from which larger molecules are made from

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2
Q

Define polymer :

A

molecules made from large numbers of monomers

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3
Q

Examples of monomers :

A

Monosaccharides
Nucleotides
Amino acids

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4
Q

Examples of polymers

A

Polysaccharides ( starch , cellulose, glycogen )
Polypeptides
Nucleic acids

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5
Q

What is a condensation reaction :

A

Joining 2 molecules together
Eliminates a water molecule
Forms a chemical bond - glycosidic bond

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6
Q

What is a hydrolysis reaction :

A

breaking 2 molecules
Required a water molecule

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7
Q

Outline the types of disaccharides and how they are formed

A

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

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8
Q

Outline Glycogen ( function, structre and structure in relation to function )

A

Function : energy stored in animal cells
Structure : alpha glucose with C1-C4 & C1-C6 glycosidic bonds

Structure in relation to its function
Branched : rapidly hydrolysed to release glucose for respiration to provide energy
Large : cannot diffuse out of cell
Insoluble in water : water potential of cell not affected

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9
Q

Outlien Starch ( function, structre and structure in relation to function )

A

Function : energy stored in plants
Structure :alpha glucose with C1-C4 & C1-C6 glycosidic bonds

Structure in relations to its function :
Helical : compact for storage in cells
Large : cannot diffuse out of cell
Insoluble in water : water potential of cell not affected

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10
Q

Outline Cellulose ( function, structre and structure in relation to function )

A

Function : provides strength and structural support to plant cells walls
Structure : beta glucose with C1-C4 glycosidic bonds

Structure related to function :
Long , straight unbranched chain
Many hydrogen bonds to form microfibrils ( strong fibers )
Hydrogen bonds are strong in high numbers
Provides strength and structural support to plant cell walls

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11
Q

Outline Benedict’s test used to identify reducing sugars

A
  1. Add benedict’s reagent(blue) to sample
    2.Heat in a boiling water bath
    3.Positive =brick red precipitate (reducing sugar present)
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12
Q

Outline non-reducing sugar test used to test for non-reducing sugars,

A

1.Add a few drops of dilute hydrochloric acid (hydrolyse sugar into its constituent reducing sugars)
2.Heat in a boiling water bath
3.Neutralize with sodium bicarbonate
4.Add Benedict’s reagent and heat again
5.Non-reducing sugar present = red precipitate

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13
Q

Outline Emulsion test for identifying fat and oils

A

1.Add ethanol to the sample to be tested, shake to mix and then add the mixture to a test tube of water
2. If lipids are present, a milky emulsion will form (the solution appears ‘cloudy’); the more lipid present, the more obvious the milky color of the solution
3. If no lipid is present, the solution remains clear

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14
Q

Outline Biuret test for identifying proteins

A

1.add iodine dissolved in potassium iodide to solution and shake/stir
2. Blue-black color = starch present

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15
Q

What are the 2 types of lipids

A

Triglycerides
Phospholipids

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16
Q

What bonds are formed with lipids and what reaction causes this ?

A
  • an ester bond is formed
  • condensation reaction causes it
17
Q

structure of triglycerides

A
  • 1 molcules of glycerol + 3 fatty acids
18
Q

Properties related to structure for triglycerides

A
  • energy storage molecules
  • 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 ( they clump together ) so no effect on water potential of cell
19
Q

Properties related to structure for phospholipids

A
  • 1 molecule of glycerol
  • 2 fatty acids
  • 3rd one is substitued by a phosphate containign group
19
Q

Properties related to structure
for phospholipids

A
  • form bilayer in cell membrane , allowing diffusion of nonpolar/ small molecules
  • Phosphate heads are polar/ hydrophilic - so are attracted to water
  • Fatty acids tails are nonpolar/ hydrophobic - so are repelled by water
20
Q

What does saturated mean with fatty acids?

A

No double carbon bonds only single in hydrocarbon chain

21
Q

What does unsaturated mean with fatty acids ?

A

One or more double carbon bond in hydrocarbon chain

22
Q

What are proteins made from ?

A

Amino acids

23
Q

What bonds are formed with proteins and what reaction causes this ?

A
  • peptide bond is formed
  • condensation reaction causes it
24
Q

Define these terms in relation to proteins : Dipeptide & Polypeptide

A

Dipeptide –> 2 amino acids joined
Polypeptie –> many amino acids joined

25
Q

Outline the process of how proteins are formed

A

Primary Structure
–> sequence of amino acids in polypepteide chains

Secondary Structure
–> hydrogen bonding between amino acids
–> causes polypeptie chains to fold into repeating patterns

Tertiary Structure
–> overall 3D Structure of polypeptides held by amino acids side chains
–> formation of ionic + hydrogen bonds + disulfide bridges

Quaternary Structure
–> some proteins are made of 2 of more polypeptide chains
–> held together by more hydrogen, ionic and disulfide bonds

26
Q

Many proteins are enzymes

Fill in the blanks :

  • Each enzyme ________ the _______ energy of the reaction it catalyses
  • Enzymes are ______ catalysts
A
  1. lowers
  2. activation
  3. biological
27
Q

What are the 2 models for enzymes

A
  • lock and key model
  • induced fit model
28
Q

Outline the lock and key model

A
  • Old and outdated
  • Active site is a fixed shape
  • Its complementary to one substrate
  • After a success collision , an enzyme substrate complex forms leading to a reaction
29
Q

Outline the Induced fit model

A
  • Recent and accepted
  • Before reaction, enzyme active sites not completely complementary to substrate/ doesn’t fit
  • Active site changed as substrate binds an enzyme substrate complex forms
  • This distorts bonds in substrate leading to a reaction
30
Q

What are the factors affecting enzyme activity

A
  • pH
  • tempreture
  • substrate concentration
  • enzyme inhibition
31
Q

Explain the effect of pH on enzyme activity ( when its the highest, when its the lowest and the result of that )

A
  • if the pH is above optimum level = rate of reaction decreases
  • enzyme denatures
  • tertiary structure and active site changes shape
32
Q

Explain the effect of tempreture on enzyme activity ( when its the highest, when its the lowest and the result of that )

A
  • increasing tempreture, rate of reaction increases, also kinetic energy increases
  • above optimum temp, rate of reation decreases
  • enzymes denature
  • tertiary structure and active site change shape
33
Q

Explain the affect of substrate concentration on enzyme activity ( when its the highest, when its the lowest and the result of that )

A
  • increasing subtratrate concentration, rate of reaction increases,
  • ## substrate concentration is a limiting factor
34
Q

Explain the affect of competitive inhibitiors on enzyme activity

A
  • decreases rate of reaction
  • has a similiar shape to substrate
  • competes/ blocks active site so substrte can bind
  • increasing substate concenration, reduces effct of inhibitors
35
Q

Explain the affect of non competitive inhibitors on enzyme activity

A

Biology AS (1 decks)

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