Biological Molecules Flashcards

(58 cards)

1
Q

Test for lipids

A

Emulsion
Add ethanol and shake to dissolve
Add water
Lipid will be milky

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2
Q

Monomer

A

Smaller units from which larger molecules are made

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3
Q

Polymers

A

Molecules made from a large number of monomers joined together

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4
Q

Lactose made up of

A

a-glucose and B-galactose

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5
Q

Sucrose made up of

A

a-glucose and a-fructose

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6
Q

Maltose made up of

A

a-glucose

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7
Q

Condensation of monosaccharides forms

A

Glycosidic bond

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8
Q

Molecular formula

A

Tells us the components of atoms and the number of each type of molecule

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9
Q

Structural formula

A

Shows how the atoms are arranged in a molecule

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10
Q

Colorimeter

A

Device used to quantify the colour by measuring transmission of absorbance

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11
Q

Glycogen

A

Energy in animals

  • a-glucose
  • branched-hydrolysis rate increased as more points of attachment so increased metabolic rate
  • 1,4 and 1,6 bonds
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12
Q

Cellulose

A

Structure in animals and plants

  • B-glucose
  • straight chains run parallel bonded by h bonds -microfibrils strong
  • 1,4 bond
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13
Q

Starch

A

Energy for plants

  • a-glucose
  • 1,6 and 1,4 bonds
  • branched-so more compact and higher rate of hydrolysis
  • can fit in a small area
  • insoluble so doesn’t effect water potential
  • large molecule so can’t pass cell membrane
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14
Q

Test for starch

A

Iodine

Orange to blue/black

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15
Q

Triglycerides made up of

A

Glycerol and three fatty acids

-condensation forms an ester bond (RCOOH)

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16
Q

R groups of fatty acids classified as

A

Saturated=no double bonds
MonoUnsaturated=one double bond
Polyunsaturated=multiple double bonds

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17
Q

Saturated fat characteristics

A
  • single bonds
  • chains are straight
  • pack closely together
  • solid at room temp
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18
Q

Unsaturated fat characteristics

A
  • double bonds
  • chains are kinky
  • molecules aren’t able to pack together
  • attractions are weak
  • liquid at room temp
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19
Q

Diff between triglycerides and phospholipids

A

One fatty acid substituted for a phosphate containing group

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20
Q

Condensation of amino acids

A

Peptide bond

Forming dipeptides or polypeptides

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21
Q

Primary protein structure

A

Sequence of amino acids

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22
Q

Secondary protein structure

A

Alpha helices or beta-pleated sheets

Formed by h bonds between amino acids

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23
Q

Tertiary protein structure

A

3D folding

  • hydrophobic R groups fold to the inner core
  • polar groups H-bond with eachother
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24
Q

Quaternary protein structure

A

Several poly peptide chains come together

25
Test for proteins
Buiret | Blue to lilac
26
Conditions that break h-bonds to cause denaturation
High temp and pH change
27
Conditions that break london forces to cause denaturation
High temp
28
Conditions that break ionic bonds to cause denaturation
Change in pH and v high temp
29
Conditions that break disulphides bridges to cause denaturation
Reducing agents
30
Conjugated protein
Contains a prosthetic group
31
Hydrogen bonds form between
Amino acids
32
Ionic bonds form between
Oppositely charged acidic and basic R-groups
33
Disulfide bridges form between
S-containing R-groups
34
Induced fit model
Collision between substrate and active site changes shape of enzyme Puts strain on the enzyme structure-stored energy Recoil of the enzyme puts strain on substrate forming and break bonds Products released as don’t fit in the active site any more
35
Enzyme conc
More active sites available More collisions More ESC formed Conc of substrate can become limiting factor
36
Substrate conc
Increases frequency of successful collisions Until all active sites are occupied Further increase in sub conc have no effect All enzymes working at max rate
37
Competitive inhibition
Fits into active site so substrate can’t bind | Some bind permanently effectively denatures the enzyme
38
Non-competitive inhibitor
Bind to the enzyme changing the shape of the active site ESC can’t form Some molecules can act as activators changing the shape of the active site to its active form
39
Temperature
Increased kinetic energy More collisions Past optimum H bonds break changing tertiary structure shape-denaturation
40
pH
H+ ions bind to -ve charged R-groups Altering H bonds and ionic bonds in 2+3 structure Change active site Active site could carry charge High h+ conc neutralises the AS charged preventing ESC being formed
41
Difference between DNA and RNA
``` DNA= Deoxyribose sugar Long chain Two chains Thymine RNA= Ribose sugar Short chain Single chain Uracil ```
42
Condensation of nucleotides
Forms phosphodiester bonds | Forming a polynucleotide chain
43
Who discovered DNA and DNA replication
Watson and Crick | By centrifuge samples with varying nitrogen
44
ATP stands for
Adenosine triphosphate
45
Hydrolysis of ATP
ATP hydrolase Releases energy by breaking a high energy bond One phosphate group broken off
46
Catabolic reactions
Makes smaller molecules
47
Anabolic
Makes larger molecules
48
Properties of water
``` Metabolite Universal solvent High Specific heat capacity Large latent heat of vaporisation Cohesion Molecular mobility Density Incompressible ```
49
Hydrogen carbonate
Regulate blood pH | Transport CO2 in blood
50
Hydroxide
Regulate blood pH
51
Nitrate
Amino acids, proteins, nucleus acid Chlorophyll Hormones Nitrogen cycle
52
Chloride
Production of urine Maintains water balance Transports CO2 in the blood HCl in the stomach
53
Phosphate
Increased rigidity in bones etc Phospholipids, ATP Regulation of blood pH Root growth
54
Potassium
``` Control of water levels Active transport Healthy leaves Nervous transmission Muscle contraction ```
55
Ammonium
Amino acids Hormones Nucleus acids
56
Sodium
Regulates osmotic Absorption of carbs in the small intestine Nervous transmission and muscles contract Turgidity in vacuole
57
Calcium
Bones, teeth cartilage Blood clotting, muscle contractions Activation of enzymes Cell wall development
58
Hydrogen
Photosynthesis, respiration Transport of O2 CO2 in blood Regulation of blood pH