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Flashcards

Biomolecules

Olivia Gniadek Concepts in Biology Tertiary Inglês 86 flashcards

Biomolecules

Flashcards do conjunto (86)

  1. 1What is a sugar?A carbonyl group (CHO)
    Multiple OH groups
  2. 2Sugars can beTrioses (3 carbon sugars)
    Pentose (5 carbon sugars e.g. ribose)
    Hexose (6 carbon sugars e.g. fructose and glucose)
  3. 3What sugars form ring structures and release water?Pentose and hexose
  4. 4What is a Carbohydrate?Carbohydrates include sugars and sugar polymers
    polymers of glucose joined together in the ß 1-4 linkage confirmation
  5. 5how does maltose formWhen glucose is joined to glucose, it forms a glycosidic linkage
  6. 6How is sucrose formedWhen fructose is joined to glucose it again forms a glycosidic linkage
  7. 7What is starcha storage unit for glucose
  8. 8What do chloroplasts makesugar
  9. 9What do monomers makeprotein
  10. 10Where can triglycerides be foundin droplets in fatty tissue that is a long carbon chain joined by using a glycerol molecule
  11. 11What is a fat?Triglycerides
    Sterols
    Phospholipids (also glycolipids)
  12. 12What are phospholipidsHave a long fatty chain like triglycerides
    They have a hydrophilic group attached to the glycerol molecule
  13. 13What is hydrophilliclikes water
    have electrically charged side chains
  14. 14What is hydrophobichates water
  15. 15What happens in the lipid bilayerhydrophilic heads are closer to the water whereas the hydrophobic tails are further away from water
  16. 16What is cholesterol needed forStabilise our membranes
  17. 17What is a protein?Proteins are made of amino acids
  18. 18What do amino acids containAn amino acid group (NH2)
    An acid group (carboxyllic acid)
    Other structures involving carbon, sulphur etc.
  19. 19What is hydrophobicity determined bynon-polar side groups
  20. 20How are polar side chains formedformed by hydroxyl groups or they will contain other amino groups
    When protonated, considered basic
  21. 21What is a polypeptide1. sequence of amino acids, proteins are joined by peptide bonds
    Secondary structure: internal bonding within polypeptide molecules
    Tertiary structure: pattern of folding conferred by hydrophilic and hydrophobic interactions within the molecular structures
    Quaternary structure: assembly of more than one polypeptide into a complex protein
  22. 22what is every fourth amino acid bonded by in the double helox of the alpha helixhydrogen
  23. 23what is the sructure of the beta pleated sheeteach sheet is parallel to another and joined by a hydrogen bond
    These two structures combined form a tertiary structure
  24. 24what forms the quartenary structureTwo large polypeptide bonds form one large protein
  25. 25What is a nucleic acid?Ribonucleic acid (RNA) - transmits instructions from DNA
    Deoxyribonucleic acid (DNA) - stores information
    Nucleic acids are polymers of Nucleotides
  26. 26What is a nucleotide1. Ring structures
    2. A 5-carbon sugar (Pentose)
    3. Phosphate (one or more)
  27. 27What forms nucleic acidsNucleotides are joined together to form polynucleotides
  28. 28What is found in RNAUracil
  29. 29What is found in DNAThymine
  30. 30Where does DNA occurNucleus
    transcribed to synthesise protein, transcribed to RNA, RNA leaves nucleus and through ribosome it is the code contained in nucleotide sequence on the mRNA. used to synthesise protein using amino acids (occurs in cytoplasm)
  31. 31What is ATPThe cells energy shuttle
    Provides energy for cellular functions
  32. 32How is energy released from ATPwhen the terminal phosphate group is hydrolysed
    ATP + H2O -> ADP + ∆G = 30.5 kJ/Mol
  33. 33What are prokaryotesBacteria, Archaea
  34. 34What are eukaryotesprotists, plants, animals and fungi
    cells are smaller and similar to prokaryotic cells
  35. 35What does a prokaryotic cell containDNA is contained in nucleoid region
    Ribosomes
    Plasma membrane
    Cell wall
  36. 36What happens in the nucleolusRibosomes are synthesised
    DNA is contained in chromatin
    (wrapped around proteins)
  37. 37What does the nuclear envelope containStructure of membrane
    Nucleus surrounded by two membranes
    Not sealed off cytoplasm
    Has pores
  38. 38What are ribosomesMade up of protein and RNA
    Large subunit and small subunit
    Synthesises protein
    Attached to the endoplasmic reticulum
  39. 39What is GolgiStacks of flattened membranous sacs; has polarity (cis and trans faces)
    Function: modifies proteins, carbohydrates on proteins, and phospholipids
    synthesis of many polysaccharides and sorting of Golgi products
  40. 40What is the function of a lysosomebreakdown of ingested substances
    Membranous sac of hydrolytic enzymes (in animal cells)
  41. 41What does the mitochondiron consist ofOuter membrane
    DNA
    Inner membrane
    Cristae
    Matrix
    Intermembrane space (essential for the transfer of energy)
    Ribosomes
  42. 42What does a plant cell containLarge central vacuole
    Large membrane-bounded vesicle
    Cell wall
    Chloroplast
    digestion, storage, water balance, cell growth and protection
  43. 43What is a chloroplastTwo membranes around a fluid stroma, contains thylakoids stacked into grana
    Function: photosynthesis
  44. 44What is an enzymeA chemial agent that speeds up a reaction without being consumed by the reaction
    An Enzyme is a catalytic protein
  45. 45What are the main functions of enzymesAccelerate reactions
    Are specific for substrates
    Are not produced or consumed in reactions
    Are proteins
  46. 46What are the functions of enzymes as catalystsThe active site can lower an EA barrier by
    Orienting substrates correctly
    Straining substrate bonds
    Providing microenvironment
    Too much hear can destroy enzyme structure
  47. 47What are cofactorsAre non-protein enzyme helpers
    Zinc
  48. 48What are co-enzymesAre organic cofactors
    Vitamins, Acetyl CoA
  49. 49What are the Inhibitors of Enzyme activityDecrease enzyme activity.
    Competitive - complete with substrate from the same binding site
    Non-competitive - bind enzyme in other location (allosteric site), altering shape
  50. 50What are the activators of enzyme activityincrease enzyme activity
    Bind to allosteric sites and keep enzymes in active configurations
  51. 51What are the competitive inhibitors of enzymesBind to active site of enzyme
    Compete with substrate
    Inhibitor binds to active site and prevents substrate binding
  52. 52What are the non-competitive inhibitors of enzymesBind to another part of the enzyme (not active site) changing the function
    Binds to enzyme at non-active site, altering conformation of enzyme to ensure active site no longer functions
  53. 53What is allosteric regulationa proteins fuction at one site is affected by the binding of a regulatory molecule at another site
    Many enzymes are allosterically regulated
    Used to control enzyme sequences
  54. 54What do obligate aerobes haveoxygen
  55. 55What do facultative anaerobes havePrefer oxygen
  56. 56What causes obligate anaerobes to dieKilled by oxygen
  57. 57where can anaerobic organisms be foundOcean sediments
    Human lower intestine and appendix
    Stomachs of ruminant animals
    Infected wounds
    Between teeth/tongue pits
  58. 58What does fermentation involveProduces ATP via substrate-level phosphorylisation
    Uses organic substance as final electron acceptor
    (e.g. pyruviate, acetaldehyde)
    Used by most organisms when o2 is limited
  59. 59What does anaerobic respiration involveelectron transport chain
    Produces ATP via oxidative and substrate-level phosphorylisation
    Uses inorganic substance as final electron acceptor (e.g. nitrate, sulphate)
    Uses mainly by bacteria in anaerobic environments
  60. 60What does aerobic respiration involveUses an electron transport chain
    Produces ATP via oxidative and substrate level phosphorylisation
    oxygen as final electron acceptor
    Used by plants, animals and prokaryotes
  61. 61What do membranes allowSeparation of cellular activities
    Gatekeeper of what enters and exits cells
  62. 62What are membranesphospholipids, proteins, sterols and carbohydrates
    Polar = like water
    Hydrophobic + hydrophilic = amphipathic
    Membranes are formed from phospholipids arranged into bilayers
  63. 63What are integral proteinspenetrate the hydrophobic core of lipid bilayer
    transmembrane proteins spanning the membrane
    Higher number of hydrophilic amino acids
    Higher number of hydrophobic amino acids
  64. 64How do you demonstrate the fluidity of membranesCells fused
    Proteins quickly mix
    Saturation of fatty acids in phospholipids of the bilayer: high saturation = decreases fluidity
  65. 65What is the role of sterolsStabilise membranes Cholesterol - reduces fluidity at moderate temperatures
    Keeps membranes fluid at low temperatures
    Increases strength
    plants use sterols to control fluidity over different temperature ranges
  66. 66Where do membrane carbohydrates formOn the surface of membrane
    Carbohydrate attached to protein = glycoprotein
    Carbohydrate attached to lipid = glycolipid
  67. 67What is the role of membrane carbohydrates in cell-cell recognitionCells bind to surface molecules on the extracellular surface the plasma membrane.
    Carbohydrates on the external side of plasma membrane vary among species, individuals and even cell types in an individual
  68. 68What are the peripheral membrane proteinsHydrophillic
    Easily washed off
  69. 69What are integral membrane proteinsAmphiphatic
    Difficult to dissolve
  70. 70What is the role of membrane carbohydratesGlycolipids, glycoproteins cell recognition
    Self' recognition
    A,B,O blood group
  71. 71What is the glycolysis cycleWhat is the glycolysis cycle
  72. 72What is the cellular respiration formulaWhat is the cellular respiration formula
  73. 73What are the steps in the citric acid cycleWhat are the steps in the citric acid cycle
  74. 74What is the photosynthesis/respiration cycleWhat is the photosynthesis/respiration cycle
  75. 75How is hydrogen extracted from bonds by DehydrogenasesHow is hydrogen extracted from bonds by Dehydrogenases
  76. 76What is the electron flow cycle in respirationWhat is the electron flow cycle in respiration
  77. 77Where does photosynthesis occurPlants, prokaryotes, algae and certain protists
  78. 78What is the difference between the action spectrum and the absorption spectrumAn action spectrum describes the wavelength of light that are the most effective at driving photosynthesis
    An absorption spectrum describes the wavelengths of light that are absorbed by pigments
  79. 79What are the two possible routes for electron flow during the light reactions of photosynthesisNon-cyclic electron flow
    Cyclic electron flow
  80. 80What is cyclic electron flowUses only Ps I
    Only generates ATP
    Active in far-red light
    Does not release O2
  81. 81What is non-cyclic electron flowUses both PS I & PS II
    Generates ATP and NADPH
    Releases O2
  82. 82What is the most abundant protein on earth?Rubisco
  83. 83What reaction does Rubisco catalyseWhat reaction does Rubisco catalyse
  84. 84What is the product of carbon fixation?3-phosphoglycerate (3 carbons) = C3 photosynthesis
  85. 85What are the three stages of the calvin cycleCarbon fixation
    Reduction
    Regeneration
  86. 86What are the inputs to the Calvin cycleMore ATP is needed than NADPH
    ATP and NADPH are produced by non-cyclic electron flow
    Extra ATP can be produced by cyclic electron flow

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Tertiary Concepts in Biology FlashCards sobre Biomolecules, criado por Olivia Gniadek em 07-05-2018.
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Olivia Gniadek
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