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3.1 Biological Molecules Flashcards

1
Q

define monomers

A

smaller units from which larger units are made

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2
Q

define polymer

A

made from larger no. of molecules joined together

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3
Q

define condensation reaction

A

joins two molecules together
formation of a chemical bond
releasing a molecule of water

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4
Q

define hydrolysis

A

breaks a chemical bond
between two molecules
involves using a water molecule

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5
Q

what are monosaccharides

A

monomers from which larger carbohydrates are made
glucose
fructose
galactose

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6
Q

how are dissacharides formed + list the equations

A

condensation of two monosaccharides
glucose + glucose = maltose
glucose + fructose = sucrose
glucose + galactose = lactose

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7
Q

draw the isomers of glucose

A

search

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8
Q

how are polysaccharides formed

A

condensation of many glucose units

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9
Q

structure + function of glycogen

A

function: energy strore in animal cells
structure: polysaccharide of a glucose
1-4, 1-6 glycosidic bonds
branched

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10
Q

structure related to function of glycogen

A

branched ; lots of active sites to be rapidly hydrolysed by enzymes for quick release of glucose for respiration for energy
large ; can’t leave cell
insoluble ; doesn’t affect water potential of cell

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11
Q

strucutre + function of starch

A

function: energy store in plant cells
structure: a glucose
made of amylose + amylopectin
amylose; 1-4 unbranched
amylopectin; 1-4, 1-6 branched

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12
Q

structure related to function starch

A

helical ; compact for storage
large; can’t leave cell
insouble; no osmostic affect on wp of cell

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13
Q

structure + function of cellulose

A

function: provides strength + structural support to plant cell walls
structure: b glucose
long, straight, unbranched cellulose chains
H bonds link parallel strands to form microfibrils
H bonds strong in numbers
provides strength + structural support to plant cells

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14
Q

benedicts test for reducing sugars

A
  • add benedict’s reagent to food sample
  • heat in boiling water bath
  • positive = brick red ppt
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15
Q

benedicts for non reducing sugars

A
  • add dilute HCL
  • heat in boiling water bath
  • neutralise with sodium bicarbonate
  • normal benedicts
  • positive = brick red ppt
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16
Q

determing glucose conc

A
  • produce dilution series of glucose conc of known conc
  • benedicts test on each sample + remove ppt
  • use calorimeter, measure absorbance, establish calibration curve
  • repeat with unknown sample + compare absorbance
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17
Q

iodine test for starch

A

add iodine dissolved in potassium iodide
shake/stir
positive = blue/black colour

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18
Q

how are triglycerides formed

A

condensation of
1 molecule of glycerol
3 molecules of fatty acids
forming an 3 ester bonds

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19
Q

the R group of a fatty acid can be

A

saturated - no c=c bond in hydrocarbon chain

unsaturated - one or more c=c bond

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20
Q

how are phospholipids formed

A

one of the fatty acids is substituted

by a phosphate group

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21
Q

emulsion test for lipids

A

add ethanol to sample
then shake
then add water
positive = milky/white emulsion

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22
Q

properties of triglycerides related to their structure

A

energy store - high ratio of c-h bonds to c atoms
release more energy than same mass of carbohydrated
insoluble in water - no effect on wp

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23
Q

properties of phospholipids related to their structure

A

form cell membrane - allowing movement of non polar/lipid soluble/small molecules down a conc gradient

24
Q

what are amino acids

A

monomers from which amino acids are made

25
what is a functional protein
may contain one or more polypeptides
26
what is the primary structure
sequence of amino acids in polypeptide chain | joined by peptide bonds
27
what is the secondary structure
h bonding between amino acids causes folding of polypetide into a helix or b pleated sheet
28
what is the tertiary structure
overall 3D structure of polypeptide further folding of polypeptide held by ionic, H bonds and DS bridges
29
what is the quaternary structure
proteins made of 2(+) polypeptide chains | held by more H, I bonds and DS bridges
30
biuret test for proteins
add biuret solution; sodium hydroxide + copper (II) sulfate blue to purple detects presence of peptide bonds
31
what do enzymes do
lowers the activation energy of reaction it catalyses speeds up rate of reaction biological catalysts
32
induced fit model
active site not completely complementary to substrate active site changes shape as substrate binds enzyme substrate complex forms stresses/distorts bonds in substrate leading to a reaction
33
explain the specificity of enzymes
specific tertiary structure + active site due to sequence of aminp acids active site is complementary to a specific substrate so only this substrate can bind to active site = enzyme - substrate complex
34
effect of enzyme conc on rate of enzyme controlled reaction
increasing enzyme conc - rate of reaction increases - enzyme conc - limiting factor - more enzymes = more active sites - more successful E-S collisions + complexes after, rate of reaction plateaus -subsstrate conc = limiting factor
35
effect of substrate conc on enzyme controlled reactions
increasing sub conc - increases rate of reaction - sub conc = limiting factor - not enough active sites - more successful E-S collisions + complexed after, rate of reaction plateaus - enzyme conc =limiting dactor - active sites saturated
36
effect of temperature on enzyme controlled reactions
increasing temp - rate of reaction increases - increase in KE - more successful E-S collisions + complexes above optimum - enzymes denature - tetiary structure + active site change shape - H and I bonds break - substrate no longer binds - enzyme denatures
37
effect of pH on enzyme controlled reaction
above/below optimum - enzymes denature - tertiary structre + active site change shape - H and I bonds break - complementary substrate no longer binds
38
effect of competitive inhibitors on enzyme controlled reactions
decrease rate of reaction - similar shape to substrate - competes for/binds to/blocks active site so substrate cant bind - fewer E-S complexes - increasing sub conc reduces inhibitor effect
39
effect of non competitive inhibitors on enzyme controlled reactions
decrease rate of reaction - binds away from active site (allosteric site) - enzyme tertiary structure/active site changes shape so substrate cant bind to active site - fewe E-S complexes - increasing sub conc has no effect on rate
40
role of DNA and RNA
DNA - holds genetic info | RNA -transfers genetic info from DNA to ribosomes
41
a condensation reaction between two nucleotides
a phosphodiester bond
42
DNA vs RNA`
DNA- deoxyribose RNA-ribose DNA-thymine RNA-uracil DNA- double stranded RNA- single stranded DNA - longer RNA- shorter
43
DNA structure
2 anit-parallel strands joined by H bonds between specific complementary base pairs
44
structure of DNA related to its function
larger no of weak H bonds between complementary bases - stable/strong double helix - protects bases/ H bonds long - stores lots of genetic info double stranded- semi conservative replication, as both strands act as templates complementary base pairing - accurate replication/identical copies coiled - compact
45
process of DNA replication
-DNA helicase breaks H bonds between bases, unwinds double helix= two strands which can act as templates -free floating DNA nucleotides attracted to exposed bases via specific complementary base pairing H bonds form -DNA polymerase joins adjacent nucleotides on new strand via condensation forming phosphodiester bonds -
46
how does DNA polymerase move
has specific shaped active site which can only bind to substrate with complementary shape only the 3' end
47
what is ATP and what is it formed of
a nucleotide derivative | molecule of ribose, adenine + 3 phosphate groups
48
ATP hydrolysis
ATP --> ADP + Pi catalysed by ATP hydrolase can be coupled to energy requiring reactions within cells -bonds between Pi bonds are high energy bonds so breaking bonds releases small amount of energy Pi released used to phosphorylate other compounds to make them more reactive
49
ATP condesation
ADP + Pi --> ATP catalysed by ATP synthase happens during respiration or photosynthesis phosphorylation of ADP
50
why is ATP a suitable source of energy
- releases energy in small,manageable amounts so no energy wasted - immediate release - cannot leave cell - quick to resynthesise
51
roles of water
metabolite in many metabolic reactions -water is reactive solvent -water is polar molecule high heat capacity - absorbs large amounts of heat before temp changes - buffers temp changes - helps maintain constant body tep large latent heat of vaporisation - absorbs large amounts of heat before evaporation - cooling effect with little loss of water via evaporation - constant body temp strong cohesion between water molecules - molecules stick together - column of water doesn't break - provides surface tension
52
where do inorganic ions occur
in solution in cytoplasm + body fluids of organisms some in high conc others in low conc each ion has specific role depending on its properties
53
phosphate ions
- attached to other molecules as a phosphate group | - form the phosphate groups of DNA/RNA nucleotides
54
hydrogen ions
maintains pH levels in body | affects rate of enzyme controlled reactions
55
iron ions
component of haem group in red blood cells transports o2 around body o2 temporarily binds to it, becomes fe3+
56
sodium ions
co transport of glucose + amino acids across cell membranes

bio (12 decks)

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