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Hint
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Answer
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what are the four types of biological molecules
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carbohydrates
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lipids
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proteins
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nucleic acids
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which molecule is made up of carbon, hydrogen, oxygen,
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lipids
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which molecule is made up of carbon, hydrogen, oxygen, nitrogen
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proteins
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which molecule contains nitrogen and phosphorus
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nucleic acids
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what is a smaller unit that combines to make a polymer
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monomer
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a large molecule made up of many repeating units of monomers joined together by chemical bonds
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polymer
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what is the process by which monomers join up to form a polymer
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polymerisation
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what type of reaction synthesises most polymers
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condensation
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what type of reaction breaks down most polymers
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hydrolysis
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A reaction where monomers join together and release a water molecule
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condensation
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A reaction where a water molecule is added to break a chemical bond between two molecules
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hydrolysis
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What is the main role of carbohydrates in living organisms
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to provide energy for cells
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what help cells identify each other and communicate
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glycoproteins
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Which carbohydrates can be used to make nucleic acids
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deoxyribose/ribose
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what are the three types of carbohydrate
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monosaccharides
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disaccharides
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polysaccharides
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name an example of a monosaccharide
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glucose/fructose/galactose
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what is the main function of disaccharides
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transport
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what is the main function of polysaccharides
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storage
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what are monosaccharides
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simple sugars
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what is the general formula for monosaccharides
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(CH2O)n
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how many carbon atoms does a pentose sugar have
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5
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what are the names of the two glucose isomers
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alpha glucose
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beta glucose
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What is the primary energy source in animals and plants
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glucose
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Why is glucose a good energy source
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soluble
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bonds store a lot of energy
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name an example of a disaccharide
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maltose/sucrose/lactose
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what is sucrose made up of
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glucose and fructose
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what are are complex carbohydrates made up of many monosaccharides joined via glycosidic bonds
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polysaccharides
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name an example of a polysaccharide
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starch/glycogen/cellulose
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what stores excess glucose and releases it to supply energy when needed (plants)
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starch
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What are the characteristics of starch that make it a good energy store
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large and insoluble/highly branched/coiled
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what stores excess glucose and releases it to supply energy when needed (animals)
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glycogen
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what consists of highly branched chains of alpha-glucose monomers joined by glycosidic bonds
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glycogen
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What are the characteristics of glycogen that make it good as an energy store
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insoluble and compact/large/more branched than starch
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what forms the structural component of plant cell walls
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cellulose
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What is the function of cellulose
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provides strength and rigidity to plant cells
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Which sugars are classified as reducing sugars
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monosaccharides and some disaccharides
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Which sugars are classified as non-reducing sugars
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polysaccharides
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How can you test for reducing sugars
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Benedict's Reagent and water bath
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What does a blue colour indicate in the reducing sugar test
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no reducing sugar present
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What does an orange colour indicate in the reducing sugar test
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medium concentration of reducing sugar
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how to determine reducing sugar concentration
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colorimeter
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How can you test for starch
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iodine solution
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what is a positive result for starch test
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blue black colour
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what is the role of lipids
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energy supply/structural components/waterproofing/insulation/protection
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What are phospholipids used as
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structural components
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What are most lipids made up of
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fatty acids combined with an alcohol
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Describe the structure of a fatty acid
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carboxyl group attached to a hydrocarbon chain
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what has a hydrocarbon chain saturated with hydrogen, with no carbon-carbon double bonds
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saturated fatty acids
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what has a hydrocarbon chain with at least one carbon-carbon double bond, causing the chain to kink
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unsaturated fatty acids
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How can you test for lipids
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ethanol shake distilled water
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What is the primary function of triglycerides
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to store energy
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What is the structure of a triglyceride
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glycerol attached to 3 fatty acid tails
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What are the components of a phospholipid
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glycerol, phosphate, 2 fatty acid tails
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What are the similarities between triglycerides and phospholipids
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contain glycerol, fatty acids and ester bond
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insoluble in water
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contain carbon hydrogen and oxygen
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What are the roles of proteins
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enzymes and antibodies/transport and structural components/hormones and muscle contraction
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What determines the properties of an amino acid
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the R group
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What type of bond joins amino acids together
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peptide bonds
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what do you call two amino acids joined by a peptide bond
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dipeptide
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Which test can identify proteins
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biuret
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What does the Biuret test detect
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presence of peptide bonds
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What does a blue colour indicate in the Biuret test
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no proteins are present
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what colour indicates present proteins
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purple
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What type of bonds are involved in the secondary structure of a protein
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hydrogen bonds
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What are the two possible shapes formed by a protein's secondary structure
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alpha helix
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beta pleated sheet
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What holds the tertiary structure of a protein together
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hydrogen and ionic bonds
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disulphide bridges
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hydrophobic and hydrophilic interactions
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What are the weak interactions between polar and non-polar R groups called
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hydrophobic and hydrophilic interactions
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which structure has two or more polypeptide chains held together by bonds
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quarternary
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What are non-protein groups added to the quaternary structure called
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prosthetic
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which structure is the unique sequence of amino acids in the polypeptide chain
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primary
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which structure is the folding of the polypeptide chain into an alpha-helix or a beta-pleated sheet
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secondary
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which structure is the complex 3D structure formed by the folding and twisting of the polypeptide chain
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tertiary
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Which type of chemical bond forms between positive and negative R groups
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ionic
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How do enzymes speed up reactions
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lower the activation energy
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what is it when a substrate(s) binds to an enzyme
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enzyme substrate complex
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What is formed during an enzyme-catalysed reaction
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products
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which enzymes act within the cells that produce them
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intracellular enzymes
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which model suggests that enzymes have a specific active site that perfectly fits the substrate(s)
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lock and key
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which model proposes that the enzyme's active site changes shape when the substrate(s) bind, putting a strain on the substrate's bonds and lowering the activation energy
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induced fit
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Name a factor that can cause an enzyme to denature
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high temperature/extreme ph
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Name factors that affect the rate of enzyme-controlled reactions
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temperature and ph/substrate and enzyme concentration
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in which solutions do H+ ions break ionic or hydrogen bonds and denature the enzymes
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acidic
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in which solutions do OH- ions break ionic or hydrogen bonds and denature the enzymes
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alkaline
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what increases the rate of reaction until eventually the rate of reaction plateaus
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increasing substrate or enzyme concentration
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what are molecules that bind to enzymes to reduce their activity
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inhibitors
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what do reversible inhibitors do
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form weak bonds with the enzyme
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what do irreversible inhibitors do
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form strong bonds with the enzyme
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what are molecules that bind to the active site of the enzyme
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competitive inhibitors
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what are molecules that bind to enzymes away from the active site
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non competitive inhibitors
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which inhibitors decrease the rate of reaction by preventing the formation of enzyme-substrate complexes
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competitive
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