Ch 5 KNOW the structures functions and importance of the 4 major types of biomolecules Dehydration lose a water molecule when you have a synthesis reaction forms a new bond Hydrolysis breaking something so you add a water molecule breaks a bond Monomers vs polymers Carbohydrates your glucose molecules give you energy Can be monosaccharaides disaccharides or polysaccharides Sugar molecules broken and formed by dehydration or hydrolysis Bond is in center ketone Bond at the end aldehyde KNOW difference between the 2 sugars DNA 1 less oxygen in DNA sugar vs RNA sugar and RNA Same molecule formula but different structure are called isomers In an enantiomer the entire structure is different Disaccharide brings two monosaccharaides by dehydration joined by glycosidic linkages Sucrose 1 and 2 Maltose 1 and 4 Polysaccharides tend to store energy Amylose not much branching of monosaccharide and amylopectin a lot of branching differ in structure itself which is branching Glycogen is an animal polysaccharide Very highly branched Differ in branching and how much energy they can store Cellulose is the main structure of polysaccharide in plants They re similar to starch But there are differences cellulose is parallel to each other and not branched They also have differences in their glucose The ring forms of their glucose alpha glucose and beta glucose are different because of the position of the hydroxyl OH molecule at the bottom or the top They re both 1 4 linkage We digest most of the starch because we can break the 1 4 alpha linkages The same enzymes in us doesn t break those cellulose 1 4 beta linkages you just excrete it Humans can t digest cellulose but animals have bacteria that help them digest it Cellulose is parallel and un branched so you can stack them on each other so they re strong Chitin structural polysaccharide Have the same beta linkages but a Nitrogen containing appendage REMEMBER the 1 2 and 1 4 linkages for disaccharide 1 molar 1000 mM Lipids energy storage and structural support with tons of insulation and cushioning for the cells One type of lipid is fat The 3 hydroxyl group from the glycerol form an ester linkage with carboxyl group you lose a water molecule to make that bond So you lose 3 water molecules to make one fat molecule Ester linkage is a compound which mixes an acid with alcohol Unsaturated liquid room temp mono has one double bond poly has many double bonds Saturated solid room temp Trans fat they add hydrogen to this form of fat all double bonds are taken away and replaced with hydrogen bonds hydrogenated fat Know the structures of carbohydrate carbon and oxygen fat carboxyl group proteins Phospholipids phosphate group glycerol 2 fatty acid chains These are the ones that make the cell membrane Hydrophilic head hydrophobic tail these are called amphipathic Sterols major one that is part of the cell membrane is cholesterol Mainly hydrophobic because it has a lot of carboxyl group Lipids phospholipids sterols fats Be able to tell if saturated unsaturated etc Proteins they are polymers of amino acid They are also refereed to as peptides Made of an amino group N 2h and carboxyl group with carbon attached to hydrogen on one end and an R molecule Tons of enantiomers carbon is asymmetric Only 20 amino acids and properties vary depending on what type of R group is attached They all have a methyl group so it s mostly non polar Cysteine has a sulfur group so it will react with water NH group and carboxyl group attached together will have a lot more polarity BE ABLE TO TELL APART WHICH WOULD BE POLAR AND NON POLAR For protein to be functional there are several level of structure Primary structure amino acid sequence secondary interactions between the backbones tertiary interactions between the side chains r chains gives you a 3d structure of the protein quaternary you can have more than one peptides interacting together Primary structure give a sequence of amino acids Secondary these interactions are made by hydrogen bonds Anything I do to get rid of hydrogen bonds will mess up the secondary structure Tertiary several bonds that can stabilize and give protein a 3D shape Know Disulfide bridge which bonds are making or breaking Quaternary results from the combo of 2 peptide structure When you change the primary structure all the others will be changed but not necessarily all will be affected Denaturation when you disrupt the protein structure There are some helpers that make sure that the proteins take the proper form and they re called Chaperonins If proteins are not folded properly they don t function properly Nucleic acids made of nucleotides made of a phosphate sugar always pentose and nitrogenous base KNOW Pyrimidine and Purines 2 ring structures Thymine is part of DNA they are all single ring structures The backbones are phosphodiester bonds they connect the nucleotides All the bond formations are from dehydration reaction synthesis Hydrogen bond is to connect purine and pyrimidine Know the complimentary based pairing A T C G SKIP SECTION 5 6 NOT ON THIS TEST 6 1 will not be on the test 6 2 don t go into details but know the cells and stuff Know the organelles and stuff Most cells are between 1 nanometer and 100nanometer Why are the cells so small It has to do something with surface area to the volume ratio How much of the surface is available to take care of the organelles inside The problem is not to increase the size but to get the organelles their supplies on time As surface area decreases it becomes bad for the cells You don t have enough surface area to take care of the volume inside Only way you grow is by dividing Small round is better than flat one Don t waste too much time on chapter 6 just know the basic structures and stuff Mitochondria chloroplasts similarity with bacteria Own DNA 2 membranes and ribosomes Endosymbiotic theory that they have similar structures to ancient prokaryotes Mutually beneficial for both organisms mitochondria in the cell The cytoskeleton basic structure of the cell Network of fibers 3 types o Microtubules tube like structure very thick Made of protein called tubulin Dimers 2 tubulins together It resists compression so it doesn t break so it is used as tracks to carry carbo They are handy for the movement of organelles and also move an entire cell example flagella and cilia They are arranged in 9 2 so they occur in doublets 9 pairs attached to 2 unfused pairs in the center Cross linking proteins hold them together You have
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