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Organic Chemistry Why Do We Eat? Carbohydrates A. Atoms – C,H,O in a 1:2:1 ratio B. Monomers – Monosaccharides Carbs Continued Examples: Monosaccharides – glucose, fructose, galactose Disaccharides – sucrose (glucose + fructose) lactose (glucose + galactose) maltose (glucose + glucose) Polysaccharides – chains of glucose (starch, glycogen, cellulose) Functions: immediate energy or short term energy storage Structure/Function Relationships Contains a lot of C-H covalent bonds that store energy We have enzymes that can break these bonds to release the energy The O-H bonds make carbs very polar so they dissolve easily and so can be move in water easily to meet up with enzymes and can be easily transported to cells and meet up with enzymes there Struc/Func Continued Even if molecules are polar – the larger the molecule – the less water soluble – harder to transport and harder for enzymes to get to and break down (also more bonds to break) Polysaccharides are more storable because more bonds and bigger Starch is made by plants – straight chains – more “packable” Cellulose is made by plants – used for structure since there are no enzymes that break it down, can bind to other cellulose chains making it stronger – called “fiber” in our diet – important for bulking up feces and cleaning intestine Glycogen is made by animals – branched so can break down quicker than starch Physiology When you eat monosaccharides, you just absorb them into the blood When you eat disaccharides and polysaccharides, you first digest them to monosaccharides so they are small enough to absorb These go to the cells to be further broken down to release the energy in them to run everything Any extra should be taken out by the liver, chained together into glycogen for longer storage then stored in the liver and muscles. Any excess carbs beyond what can be stored as glycogen get turned into fat for long term storage. Getting Ready for a Game or Contest? Which would you choose? Good Carbs vs. Bad Carbs Good – whole fruits, whole vegetables, whole grains Bad – processed carbs – white bread, pastas, white rice, any white flour product What Makes them Good or Bad? It’s all about the speed of absorption from the digestive track The speed of absorption is determined by packaging. Good vs. Bad Carbs Continued Whole fruits and vegetables – the simple sugars are encased in cellulose cell walls – hard to tear the cell walls open so it slows the absorption Whole grains and brown rice have capsule so same as above Refined flour – remove outside capsule and germ which has vitamins and important nutrients so its absorbed quickly and doesn’t have a lot of nutrients – almost all powdered starch Good vs. Bad carbs The amount a carb shoots up the blood sugar is called the Glycemic Index (GI). The higher the GI, the faster your blood sugar increases and the more unhealthy the carb is for you. Processed carbs have a high GI because the sugar is absorbed so fast, the liver can’t take all of the extra out for storage. Therefore, your blood sugar spikes. This causes you to overproduce insulin which leads to insulin resistant diabetes and other problems. Why is the Speed of Absorption Important? High GI: Sugar High/Sugar Low – feel tired, hungry, and maybe shaky. Creates insulin resistance and diabetes. Lipids Atoms – C,H,O but hardly any O (non-polar) Monomers – fatty acids (hydrocarbon chains) Examples Fats – saturated and unsaturated Cholesterol Steroid Hormones Wax Mucus Functions Long term energy storage Insulation Cushioning Protection (wax, mucous) Structure/Function Relationships Has more C-H bonds than carbs so contains a lot more energy/gram (compact energy) Had little O and is non-polar so doesn’t dissolve easily – hard to transport and hard for enzymes to get to it to break it down – can be stored for a long time Proteins Atoms: C,H,O,N (sometimes S) Monomers: amino acids Examples/Functions Fibrous Proteins For Structure Hair, teeth, nails, skin, muscles, bones, tendons, ligaments Internal structure of cells Protein Folding Video Globular Proteins Work by shape Enzymes – catalyze chemical reactions Carrier Proteins – carry oxygen to cells, transport things across membranes Receptors – receive messengers Messengers – molecules to communicate like hormones Antibodies – proteins that help kill foreign invaders Protein Channels in the cell membrane – let only certain things in or out of cells Marker Proteins – on cell surface – id’s cell as your own Fibrous vs. Globular Proteins Why is shape so important? Protein Structure/Function Relationships Fibrous – multiple polypeptides wound around each other like a rope – all of the intermolecular forces (bonds) that form between the strands makes them super strong which makes them good for building the structural parts of animals Globular – all have very intricate shapes with specifically shaped pockets on their surface which allow them to match by shape with other molecules. This makes them good for… How Proteins Fold Primary Structure – straight chain of aa – not functional – hooked together by peptide bonds which are covalent Secondary Structure – starts to fold uncharged parts start of collapse together the O of the acid groups form H bonds with the H from the amino group Spirals and curves start to form Protein Folding continued Tertiary Structure – caused by interactions of R groups that have now been brought closer together by secondary folding – Functional! Held together by: Hydrogen bonds - form between two polar R groups (most numerous) Hydrophobic interactions (water pushing non-polar groups to the inside Ionic bonds – form between a positive and a negative R group Covalent bonds – very few – form between R groups of 1 amino acid type Quarternary Structure – when more than one polypetide binds together to make the final shape of the protein (ex. Hemoglobin) – Functional! Nucleic Acids: DNA Structure? base pairing (purine/pyrimidine, A-T, G-C, covalent bonding of backbone, H bonding between bases Function? Code for proteins Copy itself before cell division Structure/function relationships? Structure/Function Why covalent bonds in backbone? In order to code for proteins – order of the bases is most imp. The order is maintained by the backbone which cannot fall apart or DNA is useless Why H bonds between base pairs? Enough to hold the 2 strands together but easy enough to sep. for replication and transcription Why purine-pyrimidine pairs Purines double ringed, pyr single ringed by pairing, all along the DNA is the same width so the covalent bonds of the backbone aren’t strained Why do we need base pairing? Ensures exact copying Structure/Function Why covalent bonds in backbone? In order to code for proteins – order of the bases is most imp. The order is maintained by the backbone which cannot fall apart or DNA is useless Why H bonds between base pairs? Enough to hold the 2 strands together but easy enough to sep. for replication and transcription Why purine-pyrimidine pairs Purines double ringed, pyr single ringed by pairing, all along the DNA is the same width so the covalent bonds of the backbone aren’t strained Why do we need base pairing? Ensures exact copying Structure/Function Why covalent bonds in backbone? In order to code for proteins – order of the bases is most imp. The order is maintained by the backbone which cannot fall apart or DNA is useless Why H bonds between base pairs? Enough to hold the 2 strands together but easy enough to sep. for replication and transcription Why purine-pyrimidine pairs Purines double ringed, pyr single ringed by pairing, all along the DNA is the same width so the covalent bonds of the backbone aren’t strained Why do we need base pairing? Ensures exact copying Enzymes Chemical reactions will not happen in living things without enzymes because we can’t produce enough energy available to get them to happen! Enzymes lower the activation energy of a chemical reaction so that it can happen at body temperature. This makes enzymes catalysts because they speed up chemical reactions How do Enzymes Work Each enzyme is different – The each have a specially shaped pocket on their surface that matches the substrate Each enzyme can only catalyze one type of chemical reaction It works basically like a lock and key Motion model of enzyme action Why are enzymes important? Because each enzyme can only catalyze one type of chemical reaction, reactions can only happen in the body where those enzymes are located. Enzymes control what chemical reactions happen where and how fast in the body so they generally run the body. Enzymes can either catalyze chemical reactions to make bonds or to break bonds “Making Reaction” The substrates go into the active site of the enzyme – it changes shape in such a way as to smash the two substrates together – they are now so close that it takes less energy to form the bond The bond now forms at regular body temperature “Breaking” Reaction The substrate goes into the active site – the enzyme changes shape in such a way as to twist the substrate out of shape – this strains one of the bonds (the one that is supposed to break) by making the atoms bonded together farther apart Now body heat is enough to finish breaking the bond How do Enzymes and Substrates Meet? Both are in motion – so random collision If they match by shape and the substrate goes into the active – the reaction will happen Things that affect enzyme activity and therefore all of the chemical reactions in a cell or body Enzyme Concentration Substrate Concentration Temperature pH Co-enzymes – vitamins – large organic molecule – fit into active site and makes the substrate fit better Co-factors – ions – fit into active site and make the substrate fit better Inhibitors Competitive – fit into active site and block the real substrate from getting in – no reaction when inhibitor is in active site Allosteric – fits into a site other than active site – changes shape of active site so it no longer works Cell signaling – signals a shape change in the enzyme so that it now becomes the right shape and activates Role of Coenzymes Allosteric Inhibitors Cell signaling and Activation of Enzymes The “Big Picture” Body makes chemical reactions optimal by maintaining the temperature and pH within the body It can make reactions happen in certain places by having enzymes there or not It can make reactions go faster by making more enzymes It can make reactions happen based on signals by signaling to make enyzmes in a certain place or to activate enzymes that are already there but not the right shape yet. If cofactor or coenzymes are needed for a reaction, they won’t work well without them If an inhibitor is present, the reaction will slow down or may not work at all