2 — molecular biology Flashcards

1
Q

describe the structure of proteins, including features that are common to all proteins and features that vary (7)

A
  • composed of one or more polypeptides
  • a polypeptide is a chain of amino acids
  • amino acids linked by peptide bonds
  • 20 different amino acids, differentiated by their R groups
  • primary structure is the sequence of amino acids in the polypeptide
  • secondary structure is the formation of alpha helices and beta pleated sheets
  • secondary structure stabilised by hydrogen bonding
  • tertiary structure is the further folding of the polypeptide
  • tertiary structure stabilised by interactions between r groups
  • fibrous or globular are the two main classes of 3D structure
  • 3D structure determined by amino acid sequence
  • quaternary structure if 2 or more poly peptides are linked to form a single protein
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2
Q

explain the roles of proteins in the movement of substances across membranes (5)

A
  • pump proteins for active transport
  • movement of particles against the concentration gradient
  • requires ATP
  • channel proteins for facilitated diffusion
  • particles diffuse along the concentration gradient
  • channel proteins allow ions to diffuse across
  • aquaporins for movement of water
  • greater membrane permeability to water with more aquaporins
  • proteins that move substances across membranes are embedded in the phospholipid bilayer
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3
Q

draw a diagram to show the ring structure of living organisms (3)

A
  • ring with 4 carbons and 1 oxygen atom
  • CH2OH attached to C4
  • OH and H attached by single bonds to C1, C2 and C3 with OH facing downwards on C2 and C3
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4
Q

outline, using graphs, the effect of different factors that influence enzyme activity (5)

A
  • enzymes have active sites that bind specific substances
  • act as catalysts to speed up reactions
  • rate increases with temperature
  • up to an optimum temperature
  • sharp decline in activity above optimum temperature
  • rate declines at a pH above and below the optimum pH
  • rate increases sharply as substrate concentration goes up
  • above a certain concentration, the rate reaches a maximum
  • competitive inhibitor present, as substrate concentration increases, enzyme requires higher concentration to achieve maximum rate
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5
Q

outline how the properties of water make it an effective coolant for the body (3)

A
  • hydrogen bonds hold water molecules together
  • evaporation requires breaking of hydrogen bonds
    water has a high heat of vaporisation
  • evaporation of water removes heat from the skin
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6
Q

describe how changes in weather conditions affect the transport and loss of water in plants (5)

A
  • water vapour lost by transpiration
  • transpiration causes transport of water in xylem
  • more water loss in hotter weather
  • because there is more heat for evaporation
  • less water loss in more humid weather
  • faster diffusion of water out of the leaf in low humidity
  • more water loss in windier weather
  • wind carries away water vapour from around the leaf
  • high winds can cause stomata closure
  • drought causes stomata to close so reduces water loss
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7
Q

outline the process of protein denaturation (4)

A
  • change to conformation
  • bonds within the protein changed
  • pH and temperature can cause denaturation
  • heat at high temperatures breaks bonds
  • extreme pH alters ionisation of amino acids and breaks ionic bonds
  • protein cannot carry out its function
  • usually permanent/ irreversible change
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8
Q

distinguish between competitive and non competitive enzyme inhibition (4)

A

competitive:
- binds to active site
- inhibitor and substrate are chemically similar
- binding of substrate prevented
- inhibition reduced by increasing substrate concentration
- useful as pharmaceuticals

non competitive:
- binding away from active site
- inhibitor different from substrate
- active site changed
- inhibition not affected by increased substrate concentration
- useful as end product inhibitors

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9
Q

draw labelled diagrams to show the structure of RNA nucleotides and how they are linked together to form a molecule of DNA (4)

A
  • ribose drawn as pentagon and labelled sugar
  • base drawn with correct link to ribose and labelled base
  • phosphate drawn with correct link to ribose and labelled P
  • two or more ribonucleotides drawn with correct link
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10
Q

identify four examples of proteins that illustrate the wide range of functions of this group of biochemicals in living organisms (4)

A
  • insulin receptors start the cellular signalling pathway
  • leptin is a hormone
  • antibodies defend body from disease
  • photosystems convert light energy to electrical impulses
  • keratin/ collagen is a structural protein
  • microtubules involved in cell division
  • ATP synthase is an enzyme that catalyses the formation of ATP
  • fibrin/ fibrinogen is a protein involved in clotting
  • haemoglobin/ sodium potassium pump is a transport protein
  • actin is involved in muscle contraction
  • spider silk is used to form spider webs
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11
Q

describe the structure of starch (5)

A
  • starch is a carbohydrate
  • starch is formed by carbon, hydrogen and oxygen
  • it is a polymer
  • formed from monosaccharides
  • linked together by condensation
  • consists of amylose and amylopectin
  • amylose is unbranched
  • amylopectin is branched
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12
Q

explain how cells produce a large variety of proteins with different sequences of amino acids (7)

A
  • protein is produced when a gene is expressed
  • genetic code consists of 4 nucleotides
  • genetic code in DNA is transcribed to mRNA
  • mRNA exits the nucleus
  • mRNA is translated into a polypeptide
  • amino acid sequence formation occurs at a ribosome
  • one codon translates to one amino acid
  • tRNA carries code for specific amino acids
  • tRNA anticodon matches with specific codon in mRNA
  • amino acids joined to form polypeptide
  • sequence of amino acids determined by order of bases
  • proteins very based on which amino acids are used and their order
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13
Q

outline how hydrogen bonds form in water (3)

A
  • water molecules are polar and dipolar
  • attractive between positive and negative poles
  • hydrogen bond formed between hydrogen and oxygen
  • bond between different water molecules
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14
Q

outline the range of functions of proteins in cells (5)

A
  • enzymes that catalyse metabolic reactions
  • proteins can be hormones which are chemical messengers to cells
  • proteins that transport through the membrane e.g. channel
  • haemoglobin in red blood cells that transports oxygen
  • membrane proteins for tissue recognition
  • structural elements of muscle fibre for movement
  • histones condense DNA into chromosomes
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15
Q

outline how hydrogen bonds form in water (3)

A
  • water molecules are polar and dipolar
  • attractive between positive and negative poles
  • hydrogen bond formed between hydrogen and oxygen
  • bond between different water molecules
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16
Q

draw a molecular diagram to show the formation of a peptide bond (3)

A
  • 2 amino acids correctly drawn
  • removal of H2O molecule shown
  • peptide bond labelled between C of C=O and N of N-H
17
Q

ADH is a peptide hormone that is produced in the hypothalamus. explain its action in the human body (8)

A
  • ADH plays a role in osmoregulation
  • acts on the collecting ducts of the kidney
  • acts in distal convoluted tubule
  • hypothalamus detects solute concentration
  • if plasma is too concentrated, pituitary releases ADH
  • ADH stimulates insertion of aquaporins in the collecting duct
  • water moves through aquaporins by osmosis into the blood
  • urine becomes more concentrated
    if blood is hypotonic, no ADH is released
    water is not reabsorbed from the collecting ducts
    urine becomes more dilute
18
Q

explain the action of enzymes in digestion and the different roles of at least two named enzymes that are produced in the pancreas (8)

A
  • enzymes catalyse/ speed up chemical reactions
  • have specific active sites to which specific substrates bind
  • enzyme catalysis involves molecular motion and the collision of substrates with the active site
  • enzymes break macromolecules into monomers in digestion
  • smaller molecules become more readily absorbed
    pancreas secretes enzymes into the lumen of small intestine
  • the small intestine has an alkaline pH
  • enzymes have maximum action at specific pHs
  • amylase breaks down starch into sugars
  • lipase breaks lipids into monoglycerides
  • protease breaks peptide bonds in proteins
19
Q

explain the importance of hydrogen bonding for living organisms (7)

A
  • cohesion in water molecules stick together
  • cohesion helps transport under tension of water
  • adhesion between water and polar molecules
  • adhesion helps water to rise in plants
  • solvent properties due to hydrogen bonds with polar molecules
  • solvent properties exemplified by glucose
  • high latent heat of evaporation so water is useful as a coolant
  • high specific heat capacity so water temperature changes less
  • base pairing between nucleotides by hydrogen bonding
  • base pairing between bases in RNA and DNA for transcription
  • proteins have hydrogen bonding in secondary structure
  • proteins have hydrogen bonding between R groups
20
Q

explain the process of photosynthesis (8)

A
  • autotrophs perform photosynthesis
  • carbon dioxide and water are the reactants
  • light splits water molecules
  • photolysis releases oxygen as a waste product
  • light energy is converted into chemical energy
  • photosynthesis produces organic compounds
  • photosynthesis occurs in chloroplasts
  • chlorophyll absorbs light
  • different pigments absorb different wavelengths of light
  • chlorophyll absorbs red and blue light
  • carbon dioxide concentration, temperature, light intensity are limiting factors
21
Q

outline the production of carbohydrates in photosynthesis (4)

A
  • light is absorbed by chlorophyll
  • light energy is converted to chemical energy
  • some of the energy is used for production of ATP
  • water molecules are split
  • produces oxygen as waste product
  • plants fix CO2
  • ATP is needed to produce carbohydrates
22
Q

distinguish between anabolism, catabolism and metabolism (3)

A
  • metabolism is all enzyme catalysed reactions in a cell
  • anabolism is the synthesis of polymers
  • catabolism is breaking down complex molecules into simpler ones
23
Q

distinguish between the structures of the different types of fatty acids in food (4)

A
  • fatty acids can be saturated or unsaturated
  • unsaturated can be monounsaturated or polyunsaturated
  • saturated fats have no double bonds
  • cis-form has hydrogen atoms on the same side of carbon double bond
  • trans-form has hydrogens on opposite sides of
  • carbon double bond
  • length of hydrocarbon chain can vary
24
Q

explain how animal cells produce the ATP that they need (5)

A
  • respiration
  • energy released from glucose
  • anaerobic respiration does not require oxygen
  • anaerobic respiration does not require oxygen
  • lactate is produced in anaerobic respiration
  • oxygen used in aerobic respiration
  • carbon dioxide and water produce in aerobic respiration
  • mitochondria used for aerobic respiration
  • larger yield of ATP from aerobic than anaerobic respiration
25
Q

explain how temperature affects enzymes (4)

A
  • speed of reaction increases as temperature rises
  • faster molecular motion so more collisions between substrate and active site
  • denaturation at higher temperatures
    active site damaged
  • an enzyme works fastest at its optimum temperature
  • inactivation at lower temperatures
  • sketch graph to model the effect of temperature on enzyme activity