13617740
Beschreibung
Karteikarten von Olivia Gniadek, aktualisiert more than 1 year ago
|
Erstellt von Olivia Gniadek
vor mehr als 6 Jahre
|
|
| Frage | Antworten |
| What is a sugar? | A carbonyl group (CHO) Multiple OH groups |
| Sugars can be | Trioses (3 carbon sugars) Pentose (5 carbon sugars e.g. ribose) Hexose (6 carbon sugars e.g. fructose and glucose) |
| What sugars form ring structures and release water? | Pentose and hexose |
| What is a Carbohydrate? | Carbohydrates include sugars and sugar polymers polymers of glucose joined together in the ß 1-4 linkage confirmation |
| how does maltose form | When glucose is joined to glucose, it forms a glycosidic linkage |
| How is sucrose formed | When fructose is joined to glucose it again forms a glycosidic linkage |
| What is starch | a storage unit for glucose |
| What do chloroplasts make | sugar |
| What do monomers make | protein |
| Where can triglycerides be found | in droplets in fatty tissue that is a long carbon chain joined by using a glycerol molecule |
| What is a fat? | Triglycerides Sterols Phospholipids (also glycolipids) |
| What are phospholipids | Have a long fatty chain like triglycerides They have a hydrophilic group attached to the glycerol molecule |
| What is hydrophillic | likes water have electrically charged side chains |
| What is hydrophobic | hates water |
| What happens in the lipid bilayer | hydrophilic heads are closer to the water whereas the hydrophobic tails are further away from water |
| What is cholesterol needed for | Stabilise our membranes |
| What is a protein? | Proteins are made of amino acids |
| What do amino acids contain | An amino acid group (NH2) An acid group (carboxyllic acid) Other structures involving carbon, sulphur etc. |
| What is hydrophobicity determined by | non-polar side groups |
| How are polar side chains formed | formed by hydroxyl groups or they will contain other amino groups When protonated, considered basic |
| What is a polypeptide | 1. 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 |
| what is every fourth amino acid bonded by in the double helox of the alpha helix | hydrogen |
| what is the sructure of the beta pleated sheet | each sheet is parallel to another and joined by a hydrogen bond These two structures combined form a tertiary structure |
| what forms the quartenary structure | Two large polypeptide bonds form one large protein |
| What is a nucleic acid? | Ribonucleic acid (RNA) - transmits instructions from DNA Deoxyribonucleic acid (DNA) - stores information Nucleic acids are polymers of Nucleotides |
| What is a nucleotide | 1. Ring structures 2. A 5-carbon sugar (Pentose) 3. Phosphate (one or more) |
| What forms nucleic acids | Nucleotides are joined together to form polynucleotides |
| What is found in RNA | Uracil |
| What is found in DNA | Thymine |
| Where does DNA occur | Nucleus 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) |
| What is ATP | The cells energy shuttle Provides energy for cellular functions |
| How is energy released from ATP | when the terminal phosphate group is hydrolysed ATP + H2O -> ADP + ∆G = 30.5 kJ/Mol |
| What are prokaryotes | Bacteria, Archaea |
| What are eukaryotes | protists, plants, animals and fungi cells are smaller and similar to prokaryotic cells |
| What does a prokaryotic cell contain | DNA is contained in nucleoid region Ribosomes Plasma membrane Cell wall |
| What happens in the nucleolus | Ribosomes are synthesised DNA is contained in chromatin (wrapped around proteins) |
| What does the nuclear envelope contain | Structure of membrane Nucleus surrounded by two membranes Not sealed off cytoplasm Has pores |
| What are ribosomes | Made up of protein and RNA Large subunit and small subunit Synthesises protein Attached to the endoplasmic reticulum |
| What is Golgi | Stacks 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 |
| What is the function of a lysosome | breakdown of ingested substances Membranous sac of hydrolytic enzymes (in animal cells) |
| What does the mitochondiron consist of | Outer membrane DNA Inner membrane Cristae Matrix Intermembrane space (essential for the transfer of energy) Ribosomes |
| What does a plant cell contain | Large central vacuole Large membrane-bounded vesicle Cell wall Chloroplast digestion, storage, water balance, cell growth and protection |
| What is a chloroplast | Two membranes around a fluid stroma, contains thylakoids stacked into grana Function: photosynthesis |
| What is an enzyme | A chemial agent that speeds up a reaction without being consumed by the reaction An Enzyme is a catalytic protein |
| What are the main functions of enzymes | Accelerate reactions Are specific for substrates Are not produced or consumed in reactions Are proteins |
| What are the functions of enzymes as catalysts | The active site can lower an EA barrier by Orienting substrates correctly Straining substrate bonds Providing microenvironment Too much hear can destroy enzyme structure |
| What are cofactors | Are non-protein enzyme helpers Zinc |
| What are co-enzymes | Are organic cofactors Vitamins, Acetyl CoA |
| What are the Inhibitors of Enzyme activity | Decrease enzyme activity. Competitive - complete with substrate from the same binding site Non-competitive - bind enzyme in other location (allosteric site), altering shape |
| What are the activators of enzyme activity | increase enzyme activity Bind to allosteric sites and keep enzymes in active configurations |
| What are the competitive inhibitors of enzymes | Bind to active site of enzyme Compete with substrate Inhibitor binds to active site and prevents substrate binding |
| What are the non-competitive inhibitors of enzymes | Bind 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 |
| What is allosteric regulation | a 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 |
| What do obligate aerobes have | oxygen |
| What do facultative anaerobes have | Prefer oxygen |
| What causes obligate anaerobes to die | Killed by oxygen |
| where can anaerobic organisms be found | Ocean sediments Human lower intestine and appendix Stomachs of ruminant animals Infected wounds Between teeth/tongue pits |
| What does fermentation involve | Produces ATP via substrate-level phosphorylisation Uses organic substance as final electron acceptor (e.g. pyruviate, acetaldehyde) Used by most organisms when o2 is limited |
| What does anaerobic respiration involve | electron 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 |
| What does aerobic respiration involve | Uses an electron transport chain Produces ATP via oxidative and substrate level phosphorylisation oxygen as final electron acceptor Used by plants, animals and prokaryotes |
| What do membranes allow | Separation of cellular activities Gatekeeper of what enters and exits cells |
| What are membranes | phospholipids, proteins, sterols and carbohydrates Polar = like water Hydrophobic + hydrophilic = amphipathic Membranes are formed from phospholipids arranged into bilayers |
| What are integral proteins | penetrate the hydrophobic core of lipid bilayer transmembrane proteins spanning the membrane Higher number of hydrophilic amino acids Higher number of hydrophobic amino acids |
| How do you demonstrate the fluidity of membranes | Cells fused Proteins quickly mix Saturation of fatty acids in phospholipids of the bilayer: high saturation = decreases fluidity |
| What is the role of sterols | Stabilise 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 |
| Where do membrane carbohydrates form | On the surface of membrane Carbohydrate attached to protein = glycoprotein Carbohydrate attached to lipid = glycolipid |
| What is the role of membrane carbohydrates in cell-cell recognition | Cells 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 |
| What are the peripheral membrane proteins | Hydrophillic Easily washed off |
| What are integral membrane proteins | Amphiphatic Difficult to dissolve |
| What is the role of membrane carbohydrates | Glycolipids, glycoproteins cell recognition Self' recognition A,B,O blood group |
| What is the glycolysis cycle | |
| What is the cellular respiration formula | |
| What are the steps in the citric acid cycle | |
| What is the photosynthesis/respiration cycle | |
| How is hydrogen extracted from bonds by Dehydrogenases | |
| What is the electron flow cycle in respiration | |
| Where does photosynthesis occur | Plants, prokaryotes, algae and certain protists |
| What is the difference between the action spectrum and the absorption spectrum | An 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 |
| What are the two possible routes for electron flow during the light reactions of photosynthesis | Non-cyclic electron flow Cyclic electron flow |
| What is cyclic electron flow | Uses only Ps I Only generates ATP Active in far-red light Does not release O2 |
| What is non-cyclic electron flow | Uses both PS I & PS II Generates ATP and NADPH Releases O2 |
| What is the most abundant protein on earth? | Rubisco |
| What reaction does Rubisco catalyse | |
| What is the product of carbon fixation? | 3-phosphoglycerate (3 carbons) = C3 photosynthesis |
| What are the three stages of the calvin cycle | Carbon fixation Reduction Regeneration |
| What are the inputs to the Calvin cycle | More ATP is needed than NADPH ATP and NADPH are produced by non-cyclic electron flow Extra ATP can be produced by cyclic electron flow |
Möchten Sie mit GoConqr kostenlos Ihre eigenen Karteikarten erstellen? Mehr erfahren.