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BU BIOL 118 - lecture 150204

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Monomers and Polymers macromolecules include proteins nucleic acids carbohydrates All are polymers made of monomers Join by condensation reaction when two monomers bond they lose a H and an OH which make water and then the two monomers have a place to bond When a protein breaks you need a H and an OH to go where the bond was so that the monomers can be neutral charge again In amino acids it s called peptide bonds the COOH group bonds with the NH3 group It s a very strong bond and not very flexible Protein Structure Primary structure the sequence of amino acids Not actually the shape of the protein The list of amino acids starts with the N terminus the amine group NH3 If you change this at all it can cause huge problems like sickle cell anemia Normal red blood cells look like tiny red donuts but with sickle cell anemia the cells look like a crescent moon The red blood cells don t move as much and can t carry as much oxygen The benefit of this is you won t get malaria Secondary structure beta pleated sheets alpha helices others caused by hydrogen bonding between amino acid backbones Beta pleated sheets are usually with short nonpolar side chain amino acids because they don t get in the way of the sheet They kind of look like an accordion Tertiary structure when you have some of the overall shape The folding is dependant on the shape and charge of the amino acids Polar side chains like to stay with polar side chains and also be on the outside where there s water Non polar side chains like to stay together and stay on the inside of the protein away from water The shape can also depend on Van der Waals forces between non polar bits and hydrogen bonds in the side chains Disulfide bonds salt bridges also make the shape It s just a bond between two sulfurs in the side chains of amino acids It s a very stable bond QuateRNAry structure sometimes proteins are made of several subunits that all have their own primary secondary structure Text table 3 1 THINGS THAT DENATURE PROTEINS temperature change pH change Protein function crucial to most tasks required for cells to exist Catalysisenzymes speed up chemical reactions Defenseantibodies and complement proteins attack pathogens Movement motor and contractile proteins move the cell or molecules with in the cell Signalingproteins convey signals between cells ex hormones Structuredefine cell shape and comprise body structures ex collagen Transportcarry materials membrane proteins control molecular movement into and out of the cell ex Lipoproteins in blood stream cholesterol is one Nucleic Acids chapter 4 3 components phosphate 2 charge sugar ribose 5 carbons number of oxygen atoms vary nitrogenous base DNA is more stable than RNA because of the fewer oxygens Purines adenine and guanine Pyrimidines cytosine and thymine and uracil Pyrimidines have a y in them in DNA Links between the nucleic acids is a phosphodiester link DNA builds from 5 to 3 because that s how RNA polymerase You can t have bonds other than c g or a t a u because the hydrogen bonds won t line up and the nucleic acids won t be able to bond and stick together If the DNA strands are not anti parallel then the hydrogen bonds won t line up and the DNA won t stay together DNA replication the DNA splits apart and DNA polymerase comes and makes new DNA by filling in the other half of the strand so you don t really have to do any guess work RNA structure usually single stranded but sometimes it will loop around and make a two stranded helix with itself and there will be a loop at one end Also can have a tertiary structure unlike DNA Tetradymena RNA makes a ribozyme Pretty reactive and can be a catalyst for reactions Carbohydrates made of monosaccharides one sugar unit Glucose food lactose galactose 2 inteRNAl structures carbonyl C O and hydroxyl OH If the CO is on the end of the chain it s an aldose If the CO is in the middle of the chain it s a ketose Most names for carbs end in ose Carbs can be linear or ring shaped They usually bond at the H and HO groups that stick out from the ring of the carb Polysaccharide types Glycogen animal storage for carbs in muscle and liver carb loading you can train your body to store a little extra glycogen by overloading on carbs pretty often Starch plant storage for carbs lots of glucoses bonded together in a helix Cellulose beta glycosidic link unlike starch and glycogen they have alpha links UNDIGESTABLE fiber in food is usually cellulose Structure is a lot of parallel strands makes cell walls often Chitin cell walls of fungi insects and crustaceans lobsters Peptidoglycan cell walls in bacteria Carb function diverse functions in cells Structural support Identity protein tags that identify cells foreign bodies lots of these are trans membrane proteins so they stick out of the cell the tag proteins are called oligosaccharides ex Blood type markers Energy starch glycogen both store glycogen


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