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SEMESTER 1 > BIO biomolecules > Flashcards

BIO biomolecules Flashcards

1
Q

what are the elements for carbohydrates?

A

carbon hydrogen and oxygen. hydrogen and oxygen is ratio of 2 hydrogen:1 oxygen

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2
Q

what groups are carbohydrates classified into?

A

3 group: monosaccharides, disaccharides and pollysaccarides

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3
Q

what are monosaccharides and disaccharides?

A

small soluble molecules easy to transport in blood and sweet to taste

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4
Q

what do monosaccharides consist of?

A

single sugars consists of triose sugars so have 3C, pentose sugars having 5C and hexose 6C.

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5
Q

what are the hexose sugars and formulas are the structures the same?

A

glucose, fructose and galactose same formula of C6H12O6 bu different structures so are isomers

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6
Q

what type of basic molecular units are the hexose sugars?

A

monomers of more complex carbohydrates

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7
Q

what are the hexose sugars used in and what type of sugars are they?

A

used in respiration to. provide energy and used in growth during formation of larger carbohydrates, all hexose sugars are reducing sugars so +ve in Benedict’s (brick red precipitate)

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8
Q

what is the difference between alpha and glucose structures and what do they form?

A

alpha the hydroxyl group is below and for beta it is above and they form different polysaccharides

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9
Q

what are disaccharides how are they joined in what reaction?

A

double sugars formed when 2 monosaccharides joined together by GLYCOSIDIC bond in a CONDENSATION reaction(so smaller molecules join together to make larger with release of water)

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10
Q

give the examples of disaccharides?

A

glucose + glucose= maltose and water
glucose and fructose= sucrose + water
glucose and galactose= lactose and water
C6H12O6 + C6H12O6= C12H22O11

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11
Q

how can a disaccharide be broken down into its monosaccharides?

A

during a HYDROLYSIS reaction (break down of larger molecule into smaller molecule by addition of water)

can be hydrolysed by boiling with acid eg dilute HCI or heating with enzyme at optimum temp

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12
Q

how would hydrolysis of sucrose work?

A

so sucrose+water would make glucose and fructose by enzyme sucrase

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13
Q

how would you use Benedict’s to test for reducing sugars?

A

all monosaccharides + disaccharides except for sucrose give +ve result

  1. small amount sample placed in test tube with 2cm^3 of benedicts solution
  2. heated in water bath for 5 mins
  3. brick red/orange colour made (made by copper I oxide) is +ve result
  4. if benedicts stays blue-no reducing sugar present
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14
Q

how would you test for non-reducing (sucrose)?

A
  1. carry out benedicts to confirm negative reresult
  2. hydrolyse another sample of sucrose by heating with dilute HCL or by using enzyme sucrase at optimum temp
  3. when cooled add dilute sodium hydroxide to neutralise acid
  4. add benedicts and heat water bath 5 mins
  5. +ve result shows non-reducing sugar was originally present
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15
Q

what are polysaccharides and the examples how are they made in what reaction?

A

large polymers of monosaccharide molecules in a chain. cellulose, starch and glycogen (all polymers of glucose)
made by joining of glucose molecule by condensation reaction

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16
Q

role of polysaccharides and arrangement?

A

differ in number and arrangement of glucose molecules, function as storage or structural molecules and relatively insoluble in water + large
non-reducing so give negative result in benedicts
unsweet to taste

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17
Q

describe cellulose where it is found and what it contains

A

-found in cell wall dividing rigidity to and shape to cell
- has 10,000 B glucose molecules joined by condensation reactions
- B1-4 glycosidic bond joining B glucose molecules together so every glucose is INVERTED
- glucose molecules form long straight chain
- OH groups which project from either side of chain form HYDROGEN bonds with OH groups of adjacent chains, making a 3-dimensional structure (microfibril)

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18
Q

what are microfibrils called when grouped into larger bundles and what direction are they in different layers?

A

-called macrofibrils
- macrofibrils in 1 layer orientated in same direction
-macrofibrils in successive layer orientated in different direction

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19
Q

how do macrofibrils provide rigidity and how is cellulose cell wall fully permeable?

A

-different layers interwoven and embedded into matrix giving rigidity
- cellulose cell wall usually fully permeable die to to minute channels between different layers of macrofibrils

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20
Q

what is starch used for?

A

it is a storage carbohydrate in plants. starch is. stored in starch grains(amyloplasts) in cytoplasm.
composed of two types amylose + amylopectin

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21
Q

describe structure of starch and what it contains?

A

-many A glucose molecules joined by condensation reactions
-in amylose + amylopectin glucose molecules make SPIRAL chain
-OH groups form hydrogen bonds with same molecules making COMPACT HELICAL CHAINS
-in amylopectin +amylose a1-4 glycosidic bonds between glucose. amylopectin has a1-6 glycosidic bonds form branch points along chain

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22
Q

what is starch hydrolysed by and what would it make?

A

starch hydrolysed by amylase
starch + water= maltose

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23
Q

where do hydrolysis reactions take place in a polymer molecule?

A

ends of a polymer molecule so more branched molecule is faster rate of hydrolysis

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24
Q

why is starch suited to its function as storage?

A

-insoluble and osmotically inactive so doesn’t draw water into cell by osmosis which may lead to cell damage

  • molecule has HELICAL shape making compact store
  • has large number of glucose molecules so abundant supply of respiratory substrate
  • too large to cross cell membrane so stays when it is made
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25
Q

what test is starch detected by?

A

iodine test
1. add 2-3 drops iodide solution (Potassium iodine)

  1. if starch present BLUE/BLACK colour is made is no starch then stays ORANGE/yellow
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26
Q

what is glycogen used for and where is it formed?

A

-storage carbohydrate in cytoplasm of animal cells + fungi
-polymer of glucose similar to starch but lots of more branches so can be hydrolysed much more rapidly to release glucose for respiration
- insoluble + osmotically inactive -ideal storage property
- stored in large amounts of LIVER + MUSCLE tissue

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27
Q

what elements does lipids contain ?

A

carbon, hydrogen + oxygen but have lower proportion of oxygen and higher hydrogen compared to caerbohdrayes

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28
Q

what are lipids used for?

A

-used in respiration and as storage and structural molecules

29
Q

why are lipids ideal storage compounds?

A

-yield twice as much energy as carbs when fully oxidised(respired)
-insoluble in water + osmotically inactive

30
Q

what do lipids consist of?

A

fats (solids) + oils (liquids) at room temp, insoluble in water but soluble in range of organic solvents eg alcohol

31
Q

what is a type of lipid and what is it made by?

A

triglycerides - joining of 3 fatty acids to one glycerol molecule during condensation reaction with loss of 3 water molecules
formular: R-COOH
R= long hydrocarbon chain and COOH is carboxylic acid group
fatty acids can be A saturated ( no double bonds) or B saturated (1 or more double bonds between c atoms)

32
Q

how can lipids by hydrolysed?

A

hydrolysed into fatty acid and glycerol by heating with acid or alkali or using enzyme LIPASE at optimum temp and pH

33
Q

what test is lipids detected by?

A

emulsion test
1. small sample in test tube with 2cm^3 ethanol
2. shake mixture so fat dissolves
3. add water in another tube and mix contents
4. while emulsion of fat droplets means lipid present

34
Q

what are phospholipids?

A

lipid with a phosphate group so phosphate group replaces 1 fatty acid molecule

35
Q

what do phospholipid consist of?

A

1 glycerol, 2 fatty acids and phosphate group in condensation reaction
phosphate molecule has polar hydrophilic head and hydrophobic tails which repel water and made of long fatty acid chains

36
Q

how are phospholipid layers made and what can they arrange themselves into?

A

when thin layer of phospholipid contact with water make a single layer as hydrophilic heads attracted to water and tails repel and project outwards

-phopholipids can arrange themselves into micelles / sheet structures

37
Q

in cell membrane what does two layers of phospholipids make?

A

bilayer present when hydrophobic tails are attracted to each other and away from water

38
Q

what elements of proteins contain and what are the sub-units(monomers) from which proteins(polymers) are made?

A

carbon, hydrogen,oxygen, nitrogen sulfur
amino acids are monomers from which proteins made

39
Q

what are amino acids made out of what do they contain and make?

A

-all amino acids have amino group and carboxylic acid group but structure of R group different
-20 different common ones
- join by condensation reactions by peptide bonds (CONH) holding them together

40
Q

what does two amino acids make and what does many amino acids make and so how many is a protein ?

A

2 = dipeptide
many = polypeptide
protein is one or more polypeptide

41
Q

how are protein hydrolysed?

A

heating with acid or using enzyme protease at optimum temp

42
Q

what are the enzymes used for proteins in hydrolysis?

A

ENDOPEPTIDASES- hydrolyse internal peptide bonds in proteins to make smaller polypeptides

EXOPEPTIDASES- remove single amino acids from ends of polypeptide chains to make dipeptides and amino acids

43
Q

what primary structure protein and what does it determine?

A

sequence of amino acids in polypeptide chain (determines specific shape of protein)

44
Q

what is secondary structure of proteins?

A
  • folding/coiling of polypeptide chain due to weak hydrogen bonding between C=O and N-H groups projecting out of peptide backbone
    -includes es alpha helix and beta pleated sheets
45
Q

what is the tertiary structure of proteins

A
  • further folding/coiling of secondary structure due to IONIC bonds, HYDROGEN bonds and DISULFIDE bridges + HYDROPHOBIC interactions
46
Q

what is quaternary structure of proteins?

A
  • highly complex proteins so one or more polypeptide chain and association of non-protein
  • held together by IONIC, hydrogen (between side chains), disulfide and hydrophobic interactions
    -eg adult haemoglobin has 4 polypeptide chains of 2 types , 2a and 2 b Rach haemoglobin has prosthetic harm group
47
Q

what are fibrous proteins and what are the structural function of?

A

structural function such as keratin in nails and collagen in bone.
- insoluble + simple tertiary + quaternary structure so long parallel polypeptide chains
- make fibres of sheets giving strength and flexibility

48
Q

what do globular proteins consists of and include eg?

A

-highly folded + coiled polypeptide chain to make compact, complex specific tertiary structure and are soluble in water .
-include enzymes, antibodies receptors and hormones

48
Q

what is the difference between globular and fibrous proteins?

A

globular and soluble meanwhile fibrous insoluble
- globular highly folded coiled polypeptide chain compact complex Tertiary meanwhile fibrous simple tertiary
- fibrous have fibrous sheets giving strength flexibility

49
Q

what type of proteins are insulin and what does it act as?

A

globular proteins hormones act as chemical messengers due to difference in primary and subsequent different tertiary structures

50
Q

how are proteins denatured and what is it caused by?

A

denaturation is alternation in tertiary structure of a protein as hydrogen bonds are broken which hold the tertiary structure together , irreversible + protein can ni longer function

-high temps above optimum breaking H bonds
- changed in pH away from optimum break hydrogen + ionic
- heavy metal ions can bind to sites n protein and rich changes in shape

51
Q

how can protein be detected by which test?

A

biuret
1. add sample to test tube with 2cm^3 buret reagent
2. purple/lilcal colour means protein present
3. if essays blue no protein present

52
Q

what type of proteins are enzymes and what do they do and what part of an enzyme determines its function?

A

globular proteins, hiu=igh molecular weight and are biological catalysts so regulate biological processes in living organisms.
tertiary structure determines specific function

53
Q

what is activation energy and how is it beneficial?

A

-activation energy minimum amount of energy needed for chemical reactions to take place
- by reducing activation energy rate of reaction increased as chemical reactions can occur with acceptable temp range

54
Q

are enzymes specific?

A

-highly specific eg like amylase act on single substrate and others such as lipase shows clear specificity for particular chemical bonds

  • its specificity is feature of unique tertiary structure of enzyme
    -structure held together by hydrogen, ionic and sometimes disulfide
  • this determines shape and electrostatic charged of active site
55
Q

what is the lock and key hypothesis of enzyme action?

A
  • active site represents small region of enzyme molecule
  • only substrate with complementary shape to active site will bind to make enzyme-substrate complex
  • reaction takes place and product is released from active site

-enzyme remains unchanged end of reaction

56
Q

what is the induced fit hypothesis?

A

-substrate interacts with active site and causes enzyme to change shape which puts strain on bonds of substrate making reaction more likely so hydrolysis

  • active site may also allow 2 molecules come very close and in a certain orientation making reaction are like eg condensation reaction
57
Q

what are the factors affecting enzyme action?

A
  1. effect of enzyme concentration

2.effect of substrate concentration

  1. effect of temperature
  2. effect of pH
58
Q

what’s the relationship between rate of reaction and concentration of enzyme and why ?

A
  • direct relationship between rate of reaction and concentration of enzyme
  • as there is more enzymes more active sites available so HIGHER probability substrate will collide with enzymes active site so rate of reaction increases
    -(which assumes amount of substrate doest limit rate of reaction)
59
Q

how does substrate concentration effect rate of reaction?

A

increasing substrate conc will increase rate of reaction to a particular point (at this point rate reaches constant value its maximum rate Vmax)

  1. rate of reaction increases as collisions between substrate and enzyme more likely
  2. rate of reaction levels out as active sites of all enzymes taken up by substrate molecules
  3. rate of reaction now LIMITED by TIME REQUIRED fir enzyme-substrate complex to form product and release it from active site. so active sites are SATURATED

4.. enzyme conc has become limiting factor

60
Q

how do enzymes work when there is an effect of temp?

A

enzymes less efficient at low temps as rate of reaction slowed down by reduced kinetic energy of reactant molecules

  1. an increase in temp provides molecules (substrate) more kinetic energy so more collisions between enzyme and substrate
  2. this increases rate of reaction up to OPTIMUM TEMP where rate of reaction is at its maximum,
  3. so increasing temp above optimum causes tertiary structure of enzyme to denature as hydrogen and ionic bonds are broken
  4. rate of reaction decreases as substrate has difficulty attaching to altered active site
  5. denaturation of protein occurs at temps above 46-50 in humans and permanent as tertiary structure is irreversibly altered
61
Q

what is temp coefficent Q10?

A

rate of reaction final +10/ rate reaction initial

62
Q

how does pH effect enzyme rate of reaction?

A

enzymes have optimum pH where rate of reaction is at a maximum
- most enzymes only active over narrow pH range
- pH very different from optimum can cause denaturation
- change in pH alters ionic charges of acidic and basic groups as they are broken tertiary structure and active site is altered
-substrate can’t bind to active site

63
Q

what can slow down rate of enzyme catalysed reactions?

A

competitive inhibitors and non competitive inhibitor

64
Q

what does competitive inhibitor do and can it be reduced ?

A
  1. inhibitor has similar molecular shape to substrate and COMPETES with it fro attachment to active site
  2. rate of reaction reduced as substrate can’t bind when inhibitor is occupying active site
  3. inhibition can be reduced by adding more substrate
65
Q

what does non-competitive inhibitor do?

A
  1. isn’t similar to molecular structure of substrate instead it combines at position other than the active site to make enzyme-inhibitor complex ALTERING tertiary structure and is altering active site of enzyme
  2. substrate can’t attach or substrate will but no product is made

3.addition of substrate will not reduce this inhibition

66
Q

what’s the difference between competitive inhibitor and non-competitive?

A

competitive is similar structure to substrate and competes by attaching but can be reduced by adding more substrate however non-competitive can’t be reduced even with more substrate as it attached to position other than active site and permanently changes tertiary structure and active site so substrate can’t attach or will but no product made

67
Q

what is end product inhibition (negative feedback)?

A

when end product of metabolic pathway begins to accumulate/increase so it may act as an inhibitor binds to allosteric site

  • so product starts to switch off on its own as production as it builds up
  • process is self-regulatory as product is used up the production is switched back on again
  • called end-prdocut inhibition and an example is negative feedback

SEMESTER 1 (7 decks)

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