Unit One Grade 12 Biology Study Notes Essay Example for Free

Unit One Grade 12 biological science Study Notes EssayLipids (Fats, phospholipids, sterols)Fatsused to insulate the body as good as protect organsSATURATED-better for you-one or more double ties among carbons-less hydrogens-oils (sunflower, flax)-lower dissolve pointUNSATURATED-worse for you-single bonds between carbons-more hydrogens-animal fats-higher melting pointsPhospholipid-2 fatty acids, 1 glycerol, inorganic phosphate group, + choline group -hydrophobic tails-hydrophilic headsPhospholipid BilayerGroupings of phospholipids move together and create a tutelar membrane with the hydrophilic heads one the out fount and very in emplacement of the kiosk and the hydrophobic tails lining one another. Sterols-4 hydrocarbon chains fused together-many functional groups impoundedCHOLESTEROL-a big part of the stall membrane cubicles turn c sand trapsterol into vitamin D and bile saltsCarbohydrates (mono, di, poly saccharides)Monosaccharides- hold cogency and store it for cellular ventilation Simple sugars provide short term vigor and storage-most common one is Glucose (C6H12O)-glactose and fructose argon chemical isomers meaning they have the same chemical formula but different structures.Disaccharides2 monosaccharides uniteglucose + glucose = maltosePolysaccharidesMany monosaccharides combined together to create STARCH, CELLULOSE and GLYCOGENStarch (amylose-simpler diagram)- long term cipher and storage Glycogen (more branched diagram) unused glucose is turned into glycogen and stored for later useCellulose- plant cells argon made of this which is why they be rigid. Used in digestion in humans, cleans out colon and intestines.Proteins building blocks of carriageAmino acids organic compound containing an aminic and a carboxyl group Have R-groups or side chains that argon responsible for how it bonds with other amino acids. The bonds between amino acids be peptide bonds. NON frigid LIKES NON POLARPOLAR LIKES POLARPOSITIVE LIKES NEGATIVEP rimary structureA bunch of amino acids wed together through and through a certain sequence coded in the DNA -the number and order of acids is specialised to each different proteinSecondary StructurePeptide chains begin to bond with each other through the r groups. Bonds done in the secondary structure are usually done between amino acids close together. This causes the polypeptide chain to become ALPHA HELIX or a BETA PLEATED SHEET-main bonds are hydrogen bonds between the carboxyl and oxygen atomsTertiary StructureMore bonds occur between amino acids but this time they are father apart from each other ca employ it to turn over and shut even more4 bondsDISULPHIDE BOND- a bond between cysteine amino acidsELECTROSTATIC BOND- an ionic bond between negative a positive side chains HYDROGEN BONDS- a bond between polar r-groupsHYDROPHOBIC INTERACTIONS- a bond between non-polar r-groupsQuatrinary StructureHighest level of organizationThe bonding of ii or more tertiary proteins, making a lot of proteins into functional proteins.Dehydration synthesis- removal of piddle and putting two blood cells together Hydrolasis- adding of water and breaking apart two molecules Redox- give an electron by = oxidized, getting an electron = reducedHomeostasisThe constant state cells try to beCertain things pass in and out of the cell at precise times and rates sothat the internal environment be stable. Concentration gradient- difference between and are of high and an field of low concentration Brownian motion- the continuous front end and collision between molecules in a liquidPassive transport requests no energySimple diffusion- the causa of molecules from an area of high to low concentration. Small uncharged molecules like oxygen are passed through the membrane of a cell easily so that the cell can have oxygen.Osmosis- movement of water across a semi permeable membrane from and area of higher concentration to an area of lower concentrationSITUATIONSFacilitated diffusio n- movement of molecules that are too big to be passed through the phospholipid bilayer or are not lipid soluble. Protiens throughout the membrane assist with the movementCarrier protiens move lonesome(prenominal) specific molecules. Bind to that molecule and go through a series of movements and shape changing to move the molecule into the cell and then goes through those steps again to return to its original shape. Channel protiens- proteins with a hole in the middle that allows bigger molecules to pass in and out of the cell.Active transport- requires extra energyCells need higher concentrations of certain nutrients to survive so sometimes molecules are moved against the concentration gradient using applied energy. moving them against the concentration gradient is active transportSodium potassium pump raft transportationNot many materials are too big to pass through the cell membrane. For those that cant, the cell membrane can wrap around the molecule to get it.Endocytosis-when the cell wraps around the molecule to absorb it-pinocytosis- cell drinking, small drop of extracellular fluid with small molecules within it (most common) -phagocytosis- cell take, large drop of extracellular fluid with organic or bacterial molecules Exocytosis-when the vesicle moves to the outside. The vesicle fixes the cell membrane and the contents are moved out of the cellCell membraneActs as a barrier for the cell, protecting the internal environment from the external environment. Cell membranes around the cell as well as around the organelles. -regulates what goes in and out of the cells and organelles4 components= phospholipid bilayer, proteins, cholesterol and carbohydratesphospholipid bilayer2 fatty acids, 1 glycerol, phosphate group, + choline group provides the physical barrierseparates the extracellular fluids from the intracellular fluidsproteinsGLOBULAR-integral= bound in the hydrophobic inner of the cell-peripheral=bound in the hydrophilic exterior of the cellFIBR OUS-figments of the cytoskeleton= microtubules creating a frame play for the membranecholesterolact as patching system and gives the cell fluiditycarbohydratescan connect to proteins (glycoproteins) or lipids (glycolipids) and act ascommunicators between cellsEnzymesBiological catalystsSpeed up reactions 1000000xReduce required reaction energyVery sensitive to their environmentWhen exposed to extreme conditions they can denature and become completely impaired Arent created nor destroyed during a reactionpH and temperature affect the activity of an enzyme because they will only work at there maximum when in the perfect conditions. Anything other than that wont be optimal and in the end cause the enzyme to denature.Enzymes are proteins with a depression called the active site. R groups stick out of the active side and rend substratums with similar R groups. The catalyzing occurs in the active site.How is the active site shape determined by the 4 levels of protein structure? -polype ptide chain- sequence of amino acids and how the r groups react with eachother which causes a shape -then they fold and bend into secondary and tertiary structure causing for the final shape -the substrate is polar so the r groups facing out into the active site have to have some sort of polarity to attract it.SIMPLE ENZYMES- enzymes made only of protein and the function results from the 3D arrangement of the amino acidsCONJUGATED ENZYMES- enzymes with both protein and non protein move a) apoenzyme- protein part of the enzymeb) cofactor-non protein part, close to active site.WITHIN A COFACTOR-coenzyme= vitamins that are altered during a reaction. These have to be replaced by unaltered molecules before a new substrate can attach -activators=minerals (metal ions)not only do environmental factors (pH and temperature) effect enzymes but substances can inhibit the actions of an enzyme.Competitive inhibiters- so similar to the substrate that they enter the active site and block the subst rate from bonding with the enzyme. This can be reversed by adding more concentration of the substrate.Non-competitive inhibiters- attach to a different part of the enzyme and cause the shape to change so the substrates cant bond correctlyAllosteric sites- some enzymes have allosteric sites a ways away from the active site. When substrates attach to it they can inhibit or simulate enzyme activity. book binding an activator to an allosteric site stabilizes the proteins conformation and leaves all active sites open. Binding an allosteric inhibitor stabilizes inactive forms of the enzyme.