Biological Molecules Flashcards

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1
Q

Water

A
  • polar molecule
  • water molecules are attracted to each other and form ‘hydrogen bonds’
  • high specific heat capacity
  • thermal E. weakens H bonds instead of increasing particles’ eK
  • a buffer against rapid temp. changes which is good for enzymes
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2
Q

Water 2

A
  • high latent heat of vaporisation
  • ^ allows organisms to cool without losing a large vol. of water e.g. sweating
  • a good solvent as it transports dissolved substances through xylem
  • water in blood plasma is vital in transferring heat around the body
  • the ‘universal solvent’ due to its polarity
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3
Q

Water 3

A
  • contains dissolved oxygen for aquatic organisms to carry out respiration
  • cohesion causes surface tension which also acts as a habitat for insects
  • cohesion allows long columns of water to travel in xylem tubes
  • less dense when a solid (ice)
  • reactant/product in metabolic reactions
    e.g. photosynthesis/aerobic respiration
    hydrolysis/condensation
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4
Q

Carbohydrates - Monosaccharides

A
  • examples; glucose, galactose & fructose
  • soluble in water due to number of hydroxyl groups (OH)
  • ^ hydrophilic molecules
  • ‘ribose’ = pentose sugar
    ‘glucose’ = hexose sugar
  • αlpha & βeta are ‘isomers’ of glucose
  • C1 hydroxyl BELOW = ALPHA
    C1 hydroxyl ABOVE = BETA
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5
Q

Disaccharides

A
  • examples; maltose, sucrose & lactose
  • produces a water molecule as H atom from one mono. bonds with hydroxyl group from the other (condensation)
  • glucose molecules are chemically bonded by glycosidic bond
  • maltose forms a 1, 4 glycosidic bond
  • adding water breaks glycosidic bond (hydrolysis)
  • sucrose = glucose + fructose
    lactose = glucose + galactose
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6
Q

Polysaccharides

A
  • glucose = store of chemical energy
  • glucose is hydrophilic so it causes water to move into cell if cell contains a lot of it by osmosis
  • ^ why plants store glucose as starch
  • starch = amylose + amylopectin
  • polymers are too large to diffuse through plasma membrane
  • enzymes are used to break glycosidic bones in starch
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7
Q

Amylose & Amylopectin

A
  • amylose = thousands of α glucose molecules joined by 1, 4 glyco. bonds
  • amylose twists into a compact helix with H bonds forming between neighbouring chains
  • hydrolysis takes place to release glucose if cell needs it
  • amylopectin branches after 25-30 glucose molecules
  • branch forms 1, 6 glycosidic bond joined to main chain
  • enzymes are at ends of branches & work rapidly due to excessive amount
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8
Q

Glycogen

A
  • the glucose storage molecule in animals (liver + muscle)
  • insoluble; so cannot diffuse out of cell
  • similar to amylopectin, however, it’s more branched it’s so more compact
  • many free ends allow enzymes to convert glycogen back to glucose rapidly
  • ^ good for animals when they rapidly require energy for respiration e.g. predator chase
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9
Q

Cellulose

A
  • polymer of beta glucose
  • unbranched polysaccharide
  • forms straight chains
  • hydroxyl groups points in different directions when side-by-side
  • every 2nd β glucose molecule flips to form 1, 4 glycosidic bonds
  • H bonds between neighbouring chains give cellulose strength
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10
Q

Cellulose 2

A
  • cellulose chains grouped together are called microfibril
  • many microfibril = macrofibril
  • many macrofibril = cellulose fibre
  • c. fibres form plant cell wall
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11
Q

3.5 Lipids

A
  • molecules in fats/oils
  • major source of energy in human diet
  • stores energy e.g. ‘adipose tissue’ under skin for insulation & around internal organs for protection
  • used for waterproofing and membrane structure
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12
Q

Triglycerides

A
  • non-polar/hydrophobic
  • 1 glycerol molecule + 3 fatty acids (3x)
  • fatty acid = carboxylic group bonded to hyrdrocarbons
  • saturated fatty acids contain single covalent bonds between carbon (C)
  • unsaturated fatty acids contain at least one double covalent bond between C
  • polyunsaturated = more than one double carbon bond
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13
Q

Triglycerides 2

A
  • glycerol = 3 hydroxyl groups + carbon + hydrogen (at ends of carbon)
  • glycerol + fatty acid = ester bond (esterification aka. condensation)
  • lipase needs 3 water molecules to break ester bonds (hydrolysis)
  • a lot of energy can be released from triglycerides
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14
Q

Phospolipids

A
  • polar/hydrophilic
  • 1 glycerol molecule bonded to 2 fatty acids + phosphate (negative)
  • heads are hydrophilic
    tails are hydrophobic
  • ^ these create a phospholipid bilayer
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15
Q

Cholesterol

A
  • sterols are not fats/oils but complex alcohol molecules
  • has a hydrophilic hydroxyl group which interacts with phospholipids heads
  • rest of molecule is hydrophobic which interacts with fatty acid tail
  • helps control fluidity of plasma membrane
  • produces bile in liver
  • makes vitamin D & steroid hormones
  • ^ these hormones can pass through plasma membranes
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16
Q

3.6 Protein Structure
Amino Acids

A
  • (amino group (NH₂)) + “HCRgroup” + carboxyl group) = general amino acid
  • Rgroup differentiates amino acids
  • dipeptide = 2 amino acids chemically bonded (peptide bond)
  • ^ condensation reaction that takes place in ribosomes
  • polypeptide = 3 or more amino acids
  • polypeptides can be hydrolysed
  • a polyP has to be folded into a 3D shape to become a functional protein
  • proteins usually contain different polyP
17
Q

Primary Structure

A
  • specific order of amino acids in a polyP
  • structure is determined by DNA sequence of gene that encodes polyP
  • changing one amino acid can affect a protein’s final structure and function
18
Q

Secondary Structure

A
  • H atoms in amino group bond with O atoms in carboxyl group
  • H bonds form between amino acids all along polyP chain causing it to twist/fold
  • 2 types called ‘alpha helix’ & ‘beta sheet’
  • H bonds hold structure in place
  • type of structure formed depends on primary structure
19
Q

Tertiary Structure

A
  • further folding of polyP due to bonds forming between R groups of a. acids
  • overall 3D shape of polyP shape
  • contains both alpha helix & beta sheet
  • critical for protein function
  • specific bonding depends on R group of amino acids
20
Q

Quaternary Structure

A
  • multiple polypeptide chains
  • e.g. haemoglobin (4 polyP chains)
  • haemoglobin has 2 subunits that are arranged to form the Q structure
  • ‘prosthetic groups’ = non-proteins that bind to protein to help carry out its role
  • ^ forms part of the structure
  • ‘haem’ is the prosthetic in haemoglobin
  • each subunit has 1 haem
  • ^ these are called ‘conjugated proteins’
21
Q

Types of Bonding

A
  1. Hydrogen bonding
    - occurs when a polypeptide has 2 amino acids with a hydroxyl group
    - bonds are easily broken by high temperatures or pH changes
  2. Hydrophobic/Hydrophilic interactions
    - amino acids with hydrophobic R groups cluster together to avoid water molecules (vice versa)
    - bonds are weak
22
Q

Types of Bonding 2

A
  1. Ionic bonding
    - occurs between amino acids with charged R groups
    - stronger than H bonds but are broken by pH changes
  2. Disulphide bridges
    - occurs between cysteine R groups
    - cysteine contains sulphur atoms which form a covalent bond
    - strongest bonds; not broken by temp/pH chages
23
Q

Globular Proteins
(Haemoglobin)

A
  • have amino acids with hydrophilic R groups on its surface so they’re soluble
  • compact & spherical
  • have functional purposes
  • forms during the tertiary structure
  • e.g. insulin, haemoglobin & catalase
  • each ‘haem’ group in haemoglobin contains a FE 2+ ion
  • ^ oxygen binds to this ion which slightly changes its quaternary structure
24
Q

Insulin

A
  • regulates blood glucose concentration
  • carries out function by binding to receptor molecules found on plasma membrane of target cells
  • precise globular shape allows it to fit into its receptor
  • PP chains are linked by disulfide bonds
  • soluble with no subunits
25
Q

Catalase

A
  • contains a ‘haem’ prosthetic group in each of its 4 subunits
  • FE 2+ ions in heam group allow catalase to interact with hydrogen peroxide
  • ^ this speeds up its break down as hydrogen peroxide is damaging to cells
  • h. perox. is a by-product of metabolism
26
Q

Fibrous Proteins

A
  • have large proportions of a. acids with H. phobic R groups so they’re insoluble
  • have structural purposes
  • not folded so not compact
  • long/narrow shape
  • unreactive; less sensitive to internal/external changes
  • examples; collagen, keratin & elastin
27
Q

Collagen

A
  • the connective tissue in skin, tendons, ligaments & nervous system
  • 3 polypeptides chains wound tightly together in a triple helix rope structure
  • polyP chain can wrap around tightly due to every 3rd a. acid being ’glycine’
  • ^ glycine has the smallest R group
  • H bonds form as polyP chains wrap around each other
  • molecule are staggered; no weak spots
28
Q

Keratin

A
  • makes up outer layer skin, hair & nails
  • insoluble in water
  • strong, inflexible molecule due to many disulphide bonds
  • nails contain more d. bonds than hair making hair “more flexible”
29
Q

Elastin

A
  • provides elastic recoil (flexibility) in alveoli & blood vessels
  • a quaternary protein made from many stretchy molecules called ‘tropoelastin’
  • contains hydrophobic regions that re-associate strands after being stretched