Biological molecules Flashcards

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1
Q

properties of water

A
  • high BP : H-bonds between water mol = lots of energy needs to evaporate water + break bonds
  • Less dense solid : H-Bonds fix positions of water mol further apart forming giant, rigid + open structure = ice floats
  • cohesive : mol attracted to one another. Plants draw water up their roots
  • adhesive : mol attracted to other materials
  • water mol are strongly cohesive = water has a skin of surface tension.
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2
Q

water for life

A
  • solvent : bc its polar - solutes can dissolve. Cytosol of euk/prokaryotes is mainly water.
  • medium for chemical reactions
  • transport dissolved compounds in and out of cells
  • efficient transport medium : cohesive = mol stick together in body
  • cohesion + adhesion = capillary action : water can rise up against a narrow tube against the force of gravity (xylem)
  • coolant : buffers temp changes during chem reactions bc of H bonds (lots of energy needed to overcome) - maintains constant temp which is imp for enzymes.
  • stable environment : doesn’t change temp easily. Ice floats forming on surface of ponds/rivers to form an insulating layer above the water - prevents aquatic organisms from dyeing due to cold weather.
  • surface tension is strong to support small insects (pond skaters)
  • water is transparent so aquatics plants can still photosynthesise - light can pass through.
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3
Q

describe glucose

A
  • monosaccharide
  • hexose
  • polar
  • soluble in water (H-bonds)
  • glucose dissolved in cytosol of cells
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4
Q

condensation reaction of glucose

A
  • two a-glucose, two hydroxyl groups interact
  • OH on C1 + C4(of other mol)
  • covalent glycosidic bond formed
  • water as by - product
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5
Q

ribose

A
  • pentose monosaccharide
  • sugar present in RNA nucleotides
  • deoxyribose present in DNA NT
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6
Q

starch

A
  • a-glucose joined by glycosidic bonds

- chemical energy store (storage mol of glucose)

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7
Q

amylose

A
  • polysaccharide in starch
  • made of glucose
  • joined by 1-4 glycosidic bonds
  • angle of bond forms a helix = stabilised by H-bonds
  • compact
  • less soluble
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8
Q

amylopectin

A
  • formed by 1-6 + 1-4 glycosidic bonds
  • branched structure
  • 1-6 branching points every 25 glucose sub units
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9
Q

glycogen

A
  • storage mol in animal + fungi
  • more branched than AP
  • more compact
  • less space needed
  • animals are mobile
  • more free ends where glucose can be added/removed
  • speeds up storing/releasing glucose required by cells
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10
Q

hydrolysis reactions

A
  • addition of water

- catalysed by enzymes

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11
Q

cellulose

A
  • b-glucose can’t join same way as a-glucose
  • OH group on C1+C4 too far apart
  • alternate b-g turn upside down
  • unable to coil/branch
  • straight chain mol formed
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12
Q

fibres from cellulose

A
  • cellulose mol form H-bonds with each other
  • forms microfibrils
  • join to form macrofibrils
  • combine to form fibres
  • fibres = strong, insoluble + in cell wall
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13
Q

why is cellulose important for diet

A
  • hard to break down into its monomers

- forms fibres necessary for healthy digestive system

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14
Q

what is a reducing sugar

A
  • all monosaccharides and some disaccharides
  • donate electrons
  • reduce another mol
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15
Q

test for reducing sugar

A
  • qualitative test
  • sample in BT
  • if solid grind/blend in water
  • add equal volume benedict’s reagent
  • gently heat in water bath for 5 mins
  • RS reacts with Cu2+ in BR
  • reduces blue Cu2+ to brick red Cu+
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16
Q

test for non-reducing

- sucrose

A
  • don’t react with benedict’s
  • solutions remains blue
  • sucrose boiled with dilute HCl
  • gives + result when warmed with BR
  • sucrose is hydrolysed by the acid
  • forms glucose + fructose = reducing sugars
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17
Q

testing for starch

A
  • potassium iodide mixed with a sample

- colour change from yellow/brown to purple/black = starch is present

18
Q

describe lipids

A
  • non-polar
  • not soluble in water
  • macromolecules = large complex + not built from repeating units
19
Q

triglyceride

A
  • combines 1 glycerole + 3 FA
  • OH groups interact
  • forms 3 water mol
  • ester bonds between FA + G
  • ## esterification = condensation
  • when TG broken down, 3H2O needed = hydrolysis

-

20
Q

saturated FA

unsaturated FA

A
  • no double bonds = saturated : all C atoms form max number of bonds with H
  • double bond = unsaturated causes mol to kick/bend so can’t pack close togethor
  • makes them liquid at R.T
21
Q

phospholipids

A
  • modified TG
  • PO43- in cytoplasm of every cell
  • have extra e- so negatively charged
  • soluble in water
  • 2 FA + phosphate head
  • non polar end (FA) and charged head (phosphate)
22
Q

phospholipid interaction with water

A
  • hydrophobic (FA) repel water
  • hydrophilic interact with water (phosphate)
  • surfactants : layer on water surface where heads in water + tails stick out
  • bilayer arrangement = forming cell membranes
23
Q

sterols

A
  • lipid
  • in cells
  • complex OH mol
  • dual hydrophilic/phobic
  • OH is polar, rest is hydrophobic
24
Q

cholesterol

A
  • is a sterol
  • in liver and intestines
  • role in CM formation
  • positioned between phospholipids
  • adds stability
  • regualtes fluidity
  • keeps fluid @ low temp and stops too fluid @ high temp
  • manufactures vitD, steroid hormones + bile
25
Q

role of lipids

A
  • form CM
  • hormone production
  • electrical insulation for impulse transmission
  • waterproofing (plants leaves + feathers)
  • thermal insulation : reduce heat loss (penguins)
  • cushioning to protect vital organs : heart + kidneys
  • buoyancy : aquatic animals (wales)
26
Q

test for lipids

A
  • emulsion test
  • mix sample with ethanol
  • mix sol with water
  • shake
  • if white emulsion layer forms on top of sol = lipid present
  • clear = negative
27
Q

amino acid structure

A
  • when amine and CA groups connected to central C react
  • OH on CA of one Aa reacts with H in amine group(NH2) of anther Aa
  • peptide bond
  • forms polypeptide (many amino acids)
  • water produced as a by products
  • condensation reaction
28
Q

forming polypeptide

A
  • several Aa joined by peptide bonds

- catalysed by peptidyl transferase in ribosomes

29
Q

primary structure

A
  • sequence of Aa
  • controlled by info in DNA
  • peptide bonds
30
Q

secondary structure

A
  • O ,H + N atoms of Aa interact
  • H-bonds form within amino acid chain
  • pulls into coiled alpha helix
    OR
  • polypeptide chains can lie parallel forming beta pleated sheet
31
Q

tertiary structure

A
  • folding of protein into final shape
    interactions:
  • hydrophilic + phobic interactions between polar + non-polar R-groups
  • hydrogen bonds - weakest
  • ionic bonds - between oppositely charged R-groups
  • disulphide bonds - strongest covalent + only between R-groups with sulphur
32
Q

quaternary

A
  • interactions of sub-units
  • identical or different sub units
  • enzymes : 2 identical
  • insulin : 2 diff subunits
  • Hb : 4 subunits
33
Q

breakdown of peptides

A
  • hydrolysis
  • protease catalyses reverse reaction
  • water mol breaks peptide bond
  • reforms amine + CA groups
34
Q

globular proteins

A
  • compact
  • water soluble
  • spherical
  • ## formed when proteins fold into tertiary structure
35
Q

insulin

A
  • globular protein
  • hormone regulates BGC
  • soluble (transp in blood)
  • precise shape to fit onto specific receptor
36
Q

conjugated proteins

A
  • globular proteins with a prosthetic group
  • metal ions/mol from vitamins
  • Haem groups = prosthetic groups : contain Fe2+
  • Catalase + Hb
37
Q

Hb

A
  • quaternary + conjugated protein
  • four poly petides , 2 alpha and 2 beta sub-units
  • each sub unit has a prosthetic haem group
  • Fe2+ combine irreversibly with O2 allow it to transport
38
Q

catalase

A
  • enzyme
  • conjugated protein
  • catalyse reactions
  • quaternary protein with 4 prosethic haem groups
  • Fe2+ allows catalse to react with H2O2 and speed up breakdown
39
Q

fibrous proteins

A
  • long , strong
  • insoluble
  • high proportion of Aa with hydrophobic R-groups
  • organised structure
  • not 3-D
  • keratin, elastin + collagen
40
Q

Keratin

A
  • fibrous
  • hair, skin , nail
  • sulphur amino acids - cysteine
  • strong disulphide bonds
41
Q

elastin

A
  • fibrous proteins
  • quaternary protein
  • in elastic fibres
  • walls of BV + alveoli
  • flexibility to expand + elastic recoil
  • made of tropoelastin
42
Q

collagen

A
  • fibrous protein
  • connective tissue
  • skin, tendons + ligaments + NS
  • 3 polypeptides wound in a long strong rope
  • flexible