Unit One Grade 12 Biology Study Notes Essay Example for Free

Unit One Grade 12 Biology Study Notes EssayLipids (Fats, phospholipids, sterols)Fatsused to insulate the body as swell up as protect organsSATURATED-better for you-one or to a greater extent double wedges between carbons-less hydrogens-oils (sunf petty(a)er, flax)-lower melting pointUNSATURATED-worse for you-single bonds between carbons-to a greater extent hydrogens-animal fats-higher melting pointsPhospholipid-2 fatty acids, 1 glycerol, phosphate group, + choline group -hydrophobic tails-hydrophilic headsPhospholipid BilayerGroupings of phospholipids move together and create a protective membrane with the hydrophilic heads one the outside and very inside of the cubicle and the hydrophobic tails facing one another. Sterols-4 hydrocarbon chemical chains fused together-many functional groups attachedCHOLESTEROL-a big part of the jail cellphone membrane cells acidulate cholesterol into vitamin D and bile saltsCarbohydrates (mono, di, poly saccharides)Monosaccharides- hold en ergy and store it for cellular respiration Simple sugars provide short term energy and storage-most general one is Glucose (C6H12O)-glactose and fructose argon chemical i aboutrs meaning they have the same chemical formula but different structures.Disaccharides2 monosaccharides combinedglucose + glucose = maltosePolysaccharides more monosaccharides combined together to create STARCH, CELLULOSE and GLYCOGENStarch (amylose-simpler diagram)- long term energy and storage Glycogen (more branched diagram) unused glucose is turned into glycogen and stored for after useCellulose- plant cells are made of this which is why they are rigid. Used in digestion in humans, cleans out colon and intestines.Proteins building blocks of lifeAmino acids constitutional compound containing an amino group and a carboxyl group Have R-groups or side chains that are responsible for how it bonds with other amino acids. The bonds between amino acids are peptide bonds. NON POLAR LIKES NON POLARPOLAR LIKES P OLARPOSITIVE LIKES NEGATIVEPrimary structureA bunch of amino acids bind together with a certain sequence coded in the DNA -the number and order of acids is specific 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 exclude together. This get downs the polypeptide chain to become ALPHA HELIX or a BETA PLEATED SHEET-main bonds are hydrogen bonds between the carboxyl and oxygen atomsTertiary Structureto a greater extent bonds occur between amino acids but this time they are father apart from each other causing it to bend and fold even more4 bondsDISULPHIDE BOND- a bond between cysteine amino acidsELECTROSTATIC BOND- an ionic bond between negative a positive side chains atomic number 1 BONDS- a bond between polar r-groupsHYDROPHOBIC INTERACTIONS- a bond between non-polar r-groupsQuatrinary StructureHighest level of organizationThe bonding of deuce o r more tertiary proteins, making a lot of proteins into functional proteins.Dehydration synthesis- removal of h2o and putting two molecules together Hydrolasis- adding of water and breaking apart two molecules Redox- give an electron away = oxidized, getting an electron = reducedHomeostasisThe constant state cells try to beCertain things drumhead in and out of the cell at specific times and rates sothat the internal environment stays stable. Concentration gradient- difference between and are of high and an area of low tightfistedness Brownian motion- the continuous course and collision between molecules in a liquidPassive transport needs no energySimple diffusion- the movement 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 buoy have oxygen.Osmosis- movement of water across a semi permeable membrane from and area of higher concentration to an area of lower concen trationSITUATIONSFacilitated diffusion- 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 movement aircraft carrier protiens move only specific molecules. Bind to that molecule and go through a series of movements and shape changing to move the molecule into the cell and and so 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. spry transport- requires extra energyCells need higher concentrations of certain nutrients to survive so sometimes molecules are moved against the concentration gradient using applied energy. lamentable them against the concentration gradient is nimble transportSodium potassium pumpBulk 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 absorb it.Endocytosis-when the cell wraps around the molecule to absorb it-pinocytosis- cell inebriety, small drop of extracellular fluid with small molecules within it (most common) -phagocytosis- cell eating, 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, protect 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= derail in the hydrophobic interior of the cell-peripheral=bound in the hydrophilic exterior of the cellFIBROUS-figments of the cytoskeleton= microtubules creating a framework for the membranecholesterolact as patching system and gives the cell liquidnesscarbohydratescan connect to proteins (glycoproteins) or lipids (glycolipids) and act ascommunicators between cellsEnzymesBiological catalystsSpeed up reactions 1000000xReduce required reaction energyVery slight to their environmentWhen exposed to extreme conditions they can denature and become completely dysfunctional Arent created nor destroyed during a reactionpH and temperature affect the bodily function of an enzyme because they will only work at there maximum when in the perfect conditions. Anything other than that wont be optimal and eventually cause the enzyme to denature.Enzymes are proteins with a depression called the active turn up. R groups stick out of the active side and attract substrates with similar R groups. The catalyzing occurs in the active site.How is the active site sha pe determined by the 4 levels of protein structure? -polypeptide 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 parts 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 repress the actions of an enzyme.Competitive inhibiters- so similar to the s ubstrate that they enter the active site and block the substrate 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. 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.