Biomolecules

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Tertiary Concepts in Biology Flashcards on Biomolecules, created by Olivia Gniadek on 07/05/2018.
Olivia  Gniadek
Flashcards by Olivia Gniadek, updated more than 1 year ago
Olivia  Gniadek
Created by Olivia Gniadek almost 6 years ago
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Question Answer
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
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