What is colorimetry used for?

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What are 5 key functions of water inside and outside of cells? What is the structure of a water molecule? How are water molecules able to hydrogen bond? What is the definition of specific heat capacity? Why do hydrogen bonds give water a high specific heat capacity? Why does water have a high latent heat of evaporation? What is the definition of cohesive? Why are water molecules cohesive? What are the advantages of water molecules being cohesive? Why is water a good solvent? Why is water less dense when it is solid? Why is water's high specific heat capacity useful for living organisms? What are carbohydrates made from? Briefly describe the structure of glucose. What are the two forms of glucose and how do they differ? What is a polymer? Briefly describe the structure of ribose? What three elements are all carbohydrates made up of? What sort of bond forms a disaccharide? Describe condensation reactions. What is maltose formed of? What do alpha-glucose and fructose join to form? 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Which part of a phospholipid is hydrophobic, and which is hydrophilic? What do bacteria use triglycerides to store? Why are triglycerides good for storage? Where are phospholipids found? What is cholesterol? What is the role of cholesterol in eukaryotic cells? Describe the shape of cholesterol. Describe the structure of a phospholipid bilayer. What are triglycerides composed of? What are proteins? What are proteins made up of? Describe the structure of an amino acid. How are amino acids joined together? What sort of reaction joins amino acids together? What reaction breaks a peptide bond? What are the four levels of protein structure? What is the primary structure of proteins? What is the secondary structure of proteins? What sort of bonds are formed in the secondary structure of proteins? What is the tertiary structure of a protein? What is the quaternary structure of a protein? What bonds are involved in the tertiary structure of a protein? What are disulfide bonds? What happens when a protein is heated up to a high temperature? Describe the structural properties of a globular protein. What is a globular protein? What is the role of haemoglobin? What does it mean to be a conjugated protein? Describe the structure of haemoglobin. What is the role of insulin? What organ secretes insulin? Describe the structure of insulin. What is amylase? Describe the structure of amylase. What are fibrous proteins? What is the role of collagen? What is the structure of collagen? What is keratin? What is the structure of keratin? What is elastin? What is the structure of elastin? What is the general structure of an amino acid? What are inorganic ions? What is the difference between a cation and an anion? What is the role of calcium in biological processes? What is the role of sodium in biological processes? What is the role of potassium in biological processes? What is the role of hydrogen in biological processes? 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What sort of reaction breaks down polynucleotides? What bonds form between two DNA polynucleotide strands? What does complementary base pairing mean? Which DNA base does adenine always pair with? Which DNA base does cytosine always pair with? How many hydrogen bonds form between adenine and thymine? How many hydrogen bonds form between cytosine and guanine? What does antiparallel mean? What sort of reaction purifies DNA? What is DNA helicase? Describe how DNA self-replicates. What is semi-conservative replication? What can a random mutation lead to? What is meant by an anticodon? What is the role of tRNA during translation? What is the role of mRNA during translation? What is the product of translation? When does RNA polymerase stop making mRNA? What are enzymes? What is meant by the phrase "biological catalyst"? Give an example of an intracellular enzyme. When is hydrogen peroxide formed? What is the role of catalase? Give examples of extracellular enzymes. What is the role of amylase? What is the role of trypsin? What are globular proteins? Describe the structure of an enzyme. What is meant by an active site? What determines the specific shape of an enzyme's active site? What does the shape of the substrate need to be in relation to the active site of an enzyme? What does a reduction in activation energy mean? What is activation energy? How does the formation of an enzyme-substrate complex lower the activation energy? What is the lock and key model? Why might the lock and key model be incorrect? What is the induced fit model? How does the induced fit model explain the specificity of enzymes? How does temperature influence enzyme activity? What happens if temperature of an enzymatic reaction gets too high? What is meant by an enzyme being denatured? What is meant by the optimum temperature? What is the optimum temperature of most human enzymes? What is the temperature coefficient? How can the temperature coefficient be measured? What is the rough Q10 value of most enzyme-controlled reactions? What is meant by an optimum pH value? What would the optimum pH value of pepsin most likely be? What factors make substrate molecules more likely to collide with enzymes in solution? How does enzyme concentration affect the rate of reaction? How does substrate concentration affect the rate of reaction? How does the rate of reaction change over time when substrate concentration decreases? How can the effects of temperature, pH, enzyme/substrate concentration be investigated experimentally? What is meant by an independent variable? What is meant by a dependent variable? What does it mean if an enzyme is denatured? Explain why increasing the concentration of an enzyme does not always increase the rate of reaction. Explain the effect of increasing substrate concentration on the rate of an enzyme-catalysed reaction. Suggest two methods of measuring the rate of an enzyme catalysed reaction. What are cofactors? What are co-enzymes? What do cofactors do? What ion is a cofactor for amylase? How do coenzymes differ from cofactors? Is a vitamin a cofactor or a coenzyme? What do cofactors do? What is a tightly bound cofactor known as? What is the prosthetic group for carbonic anhydrase? What is the role of enzyme inhibitors? What is competitive inhibition? What shape do competitive inhibitors have? During competitive inhibition, what impacts how much the enzyme is inhibited? What does increasing the concentration of substrate do during competitive inhibition? What is non-competitive inhibition? What does a non-competitive inhibitor do to the active site of an enzyme? What effect on rate of reaction does an increase in substrate concentration do during non-competitive inhibition? What is the allosteric site? What is the difference between reversible and non-reversible inhibitors? What sort of bonds are involved in irreversible enzyme inhibition? What sort of bonds will be involved in reversible enzyme inhibition? Give examples of medicinal drugs as enzyme inhibitors. Give examples of metabolic poisons that act as enzyme inhibitors. What is cyanide an irreversible inhibitor of? What is malonate an enzyme inhibitor of? What is arsenic an enzyme inhibitor of? How are metabolic pathways regulated? What is end-product inhibition? Is end-product inhibition reversible? How can enzyme inhibition help protect cells? What is the difference between competitive and non-competitive enzyme inhibitors? Why are some enzymes synthesised as inactive precursors?