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T1 bio mols Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

what is a monomer

A

smaller, repeating unit from which larger polymers are made

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2
Q

what is a polymer

A

large mols made from many repeating monomer units joined together in a chain (polymerisation)

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3
Q

what is a condensation reaction + example

A

monomers joining together with the removal of a water mol
eg monosaccharides condense to form a polysaccharide

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4
Q

what is a hydrolysis reaction + example

A

breaking of chemical bonds between 2 mols to split a polymer to its constituent monomers w the addition of water
eg. polysaccharides hydrolyse to form monosaccharides

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5
Q

what kind of bonds join carbohydrates

A

glycosidic bonds between 2 hydroxyl -OH groups - formed in condensation reactions

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6
Q

def + examples of reducing sugars

A

sugars that can donate electrons
-glucose
-fructose
-galactose

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7
Q

def + example of non-reducing sugar

A

sugar cant donate electrons
-sucrose

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8
Q

properties of monosaccharides

A

-white, crystalline solids at room temp
-soluble in water
-sweet
-all are reducing sugars

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9
Q

test for reducing sugars

A
  1. add benedicts (blue)
  2. BOIL in water bath
  3. Brick red colour (can be on scale depending on conc)
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10
Q

maltose =

A

glucose + glucose

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11
Q

sucrose =

A

glucose + fructose

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12
Q

lactose =

A

glucose + galactose

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13
Q

test for non-reducing sugars

A
  1. add dilute HCl
  2. BOIL in water bath
  3. neutralise w sodium hydrogen carbonate. test pH
  4. add benedicts and BOIL
  5. blue to brick red
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14
Q

structure of starch

A

2 long alpha glucose chains:
1. Amylose -
- unbranched, helix-shaped chain wound into coil
-1,4 glycosidic bonds

  1. Amylopectin -
    -branched chain - easy hydrolysis for resp
    -1,4 and 1,6 glycosidic bonds
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15
Q

test for starch

A
  1. add orange/brown iodine in potassium iodide solution
  2. blue black
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16
Q

structure of glycogen

A
  • alpha glucose chains
    -1,4 glycosidic bonds
    -highly branched - compact, easily hydrolysed
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17
Q

structure of cellulose

A

-beta glucose
-1,4 glycosidic bonds
-every other monomer is INVERTED
-H bonds form between chains increasing strength

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18
Q

structure of trigylcerides

A
  • 3 fatty acid chains and 1 glycerol
  • ESTER bond between hydroxyl group (on glycerol) and carboxyl group (on fatty acids)
  • can be saturates (NO double C bonds) or unsaturated (HAS double C bonds)
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19
Q

functions of triglycerides

A

-source of energy: high ratio of energy-story C-H bonds, release energy used to produced ATP when oxidised
-storage mol - low mass to energy ratio
-insulation - part of myelin sheath around nerve fibres and part of blubber in whales

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20
Q

structure of phospholipids

A

-glycerol, 2 fatty acid chains, phosphate mol
-ESTER bond
-hydroPHOBIC tails
-hydroPHILIC heads

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21
Q

functions of phospholipids

A

-form cell-surface membranes (phospholipid bilayer) - barrier between inside and outside of cell - allows diff conditions
-contribute to fluidity of membrane - mainly saturated fatty acids = less fluid
-form micelles when in contact w water

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22
Q

test for lipids

A

-emulsion test
1. add ethanol to sample and shake to dissolve lipids
2. add to water and shake gently
3.cloudy-white emulsion forms on top = pos result

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23
Q

structure of amino acids

A
  1. amine group (NH2)
  2. carboxyl group (COOH)
  3. hydrogen atom
  4. central C atom
  5. variable R group - every amino acid has diff chemical on R group
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24
Q

primary structure of proteins

A

-sequence of amino acids determined by DNA
-mutations can lead to beneficial new features

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25
Q

secondary structure of proteins

A

-proteins can form 2 shapes: alpha helix or beta pleated sheet
-determined by type of H bonding that occurs

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26
Q

tertiary structure of proteins

A

-now functional
-3D shape formed from further folding
-bonds form to maintain structure:
1. disulphide bridges - between sulphur in R groups
2. hydrogen bonds - numerous and easily broken
3. ionic bonds - between carboxyl and amine groups that arent involved in peptide bonds

27
Q

quaternary structure of proteins

A

-more than 1 tertiary protein chain joined together
-may contain prosthetic (non-protein) group eg. Haemoglobin has iron ions

28
Q

test for proteins

A
  1. add biurets solution (sodium hydroxide and copper sulphate)
  2. blue to purple =pos result
29
Q

2 basic types of protein

A
  1. globular - metabolic function - eg. haemoglobin, enzymes
  2. fibrous - structural function - eg. collagen in skin
30
Q

structure of enzymes

A

-globular proteins
-have functional active site that forms small depression within larger enzyme mol
-active site has relatively low no of amino acids

31
Q

function of enzymes

A

-act as catalysts - increase RoR without undergoing permanent changes themselves
-can be used repeatedly so are effective in small amounts

32
Q

induced fit model

A

-when specific enzymes and substrates bind, the enzyme changes shape so that they can form an enzyme-substrate complex
-it does this by breaking bonds in the enzymes tertiary structure during the distortion of the active site

33
Q

how do enzymes increase RoR

A

-when the enzyme changes shape as an enzyme-substrate complex forms (induced fit model), the bonds in the enzymes tertiary structure break
-this LOWERS activation energy
-increases RoR as it takes less energy for reactions to occur

34
Q

4 factors affecting rate of enzyme-controlled reactions

A
  1. temp
  2. pH
  3. enzyme conc
  4. substrate conc
35
Q

how does temp affect RoR

A

-RoR increases up to the optimum temp
-Ek of the enzyme increases, increasing collisions w the enzyme active sites
-above optimum temp, RoR slows as enzymes become denatured. below optimum temp, RoR slows as Ek is decreased

36
Q

how does pH affect RoR

A

-pH of solution is measure of hydrogen ion conc
-enzymes have an optimum pH - become denatured at extremes of pH
-below or above optimum, solutions w an excess of H+ or OH- ions can cause the H and ionic bonds that hold the tertiary structure of enzymes together to break, altering the shape of the active site

37
Q

how does enzyme conc affect RoR

A

-higher enzyme conc increases RoR - greater no of active sites and greater likelihood of enzyme-substrate complex formation
-as long as there is sufficient substrate conc, RoR increases proportionally to enzyme conc

38
Q

how does substrate conc affect RoR

A

-higher substrate conc increases RoR up to a point (if enzyme conc is fixed)
-will reach a point where all active sites are full and RoR will plateau

39
Q

competitive enzyme inhibitors

A

-have similar shape to that of substrate mols so can fit into active sites and prevent actual substrate mols from forming enzyme-substrate complexes

40
Q

non-competitive enzyme inhibitors

A

-bind to allosteric site (any site that isnt active site), changing shape of whole enzyme and indirectly distorting active site, preventing enzyme-substrate complexes being formed
-if only slight change occurs, activation energy may just be increased

41
Q

effect of adding more substrate on competitive enzyme inhibitors

A

-effect of competitive inhibitors decreased - substrate more likely to collide w active site and form enzyme-substrate complex

42
Q

effect of adding more substrate on non-competitive enzyme inhibitors

A

-effect of non-competitive inhibitors is constant, even if more substrate is added
-shape of active sites remains changed and enzyme-substrate complexes are still unable to form

43
Q

calculating pH equation

A

pH = -log₁₀ [H⁺]

44
Q

role of hydrogen ions

A

-lower pH of substances (make them more acidic)
-can regulate pH of body fluids to enable enzyme activity

45
Q

role of iron ions

A

-component of haemoglobin that transports oxygen
-involved in transfer of electrons during photosynthesis and respiration

46
Q

role of sodium ions

A

-involved in co-transport of glucose and amino acids.
-have role in generating action potentials

47
Q

role of phosphate ions

A

-component of DNA, RNA and ATP
-increase reactivity of ADP
-found in phospholipids in cell membranes

48
Q

name the inorganic ions (brief)

A
  1. hydrogen
  2. sodium
  3. iron
  4. phosphate
49
Q

properties of water (brief)

A

-dipole (2 different charges)
-metabolite
-solvent
-high specific heat capacity
-high latent heat of vaporisation
-high surface tension
-high cohesion = capillary action

50
Q

structure of ATP

A

-adenosine triphosphate
-Adenine, ribose and 3 phosphate molecules

51
Q

role of ATP and 4 processes it is involved in

A

-energy-carrying mol that provides constant supply of immediate energy to drive processes such as:
1. anabolic reactions
2. active transport
3. energy for muscle contraction
4. conduction of nerve impulses

52
Q

hydrolysis of ATP

A

-terminal phosphate is removed and remaining molecule becomes ADP.
-removed phosphate called Inorganic Phosphate (Pi).
-reaction catalysed by ATP hydrolase
-bonds between P groups are unstable so have low activation energy and are easily broken
-release large amount of energy when bonds are broken

53
Q

synthesis of ATP

A

-ADP combined w an inorganic phosphate (Pi)
-catalysed by enzyme ATP synthase in condensation reaction that requires energy
-made during respiration and photosynthesis
-can also be made when P groups are transferred from donor molecules (substrate-linked phosphorylation)

54
Q

what did Watson and Crick come up w

A

-semi-conservative DNA replication theory

55
Q

what did Meselsohn and Stahl prove

A

-Watson and Crick’s semi-conservative DNA replication theory

56
Q

how was semi-conservative DNA replication proven

A
  1. labelled original DNA mol by growing it on medium of Nitrogen-15 (heavier)
    2.transferred bacteria to medium of Nitrogen-14 and allowed single gen to replicate
    3.spun new DNA in centrifuge to determine mass - if semi-conservative rep had taken place, all DNA mols would contain both heavy N-15 and light N-14 and would settle in middle of tube
57
Q

what is semi-conservative DNA replication

A

-only 1 strand is newly made and the other is pre-existing and acts as a template for the other strand to be formed (due to base pairings)
-ensures genetic continuity between gens of cells to make sure they can perform same role as parent cell

58
Q

process of semi-conservative replication

A
  1. enzyme DNA helicase breaks H bonds between bases and separates strands
  2. each exposed polynucleotide strand acts as a template for new complementary free nucleotides to bind to specific base pairing
  3. enzyme DNA polymerase joins strands together in condensation reactions
  4. each new DNA mol contains one strand from parent and 1 new strand (half of DNA has been conserved)
59
Q

RNA structure

A

-phosphate group, ribose, nitrogenous base (Adenine, Cytosine, Guanine, Uracil)
-single stranded polynucleotide w nucleotides joined by phosphodiester bonds
-bond is between ribose sugar of 1 nucleotide and phosphate group of next

60
Q

what are the 3 types of RNA (brief)

A
  1. messenger RNA (mRNA)
  2. transfer RNA (tRNA)
  3. ribosomal RNA (rRNA)
61
Q

DNA properties and adaptations

A

-extremely stable due to phosphodiester backbone protecting chemically reactive bases inside double helix - means DNA rarely mutates and can copy info from gen to gen w minimal change

-H bonds link base pairs, meaning strands are easy to break during replication/protein synthesis

-large mols so can carry huge amounts of info

62
Q

what are purines + example

A

-make 2 H bonds
-double ringed structures
-adenine and guanine

63
Q

what are pyrimidines + examples

A

-make 3 H bonds (more stable)
-single ringed structure
-thymine, cytosine and uracil

64
Q

DNA structure

A

-phosphate group, deoxyribose and a nitrogenous base (adenine, guanine, cytosine, thymine)
-nucleotides joined by phosphodiester bonds between sugar and phosphate group
-sugar and base joined by glycosidic bonds
-strands run in opposite directions (antiparallel)

Biology (6 decks)

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