MCB 150: EXAM I
MCB 150: EXAM I MCB 150
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This 11 page Study Guide was uploaded by Jessica Logner on Sunday May 8, 2016. The Study Guide belongs to MCB 150 at University of Illinois at Urbana-Champaign taught by Bradley G Mehrtens in Summer 2015. Since its upload, it has received 28 views. For similar materials see Molecular and Cellular Biology in Molecular, Cellular And Developmental Biology at University of Illinois at Urbana-Champaign.
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Date Created: 05/08/16
MCB 150 EXAM I eukaryote cell containing a nucleus and specialized organelles prokaryote cell without a true nucleus major features found in all types of cells nucleoid region, cytoplasm, plasma membrane, ribosomes three domains of life bacteria, archae, eukaria horizontal gene transfer organism in one domain swaps or shares information with organism in another domain three tenants of cell theory cell is the fundamental unit of life, every living thing is made of one or more cells, all cells come from preexisting cells resolution the ability to identify two close objects as seperate why are cells small? surface area to volume ration are ribosomes considered organelles? no, not membrane bound cell wall protect the cell, maintain its shape and prevent uptake or loss of water. not found in animal cells flagella threadlike structures protruding from cell, used in locomotion vesicles sacs used to store and transport materials chromosomes tightly packed DNA central vacuole found in plant cells, used to store proteins, pigments and waste nucleus center of genetic information, surrounded by phospholipid bilayer membrane ribosomes synthesize proteins rough endoplasmic reticulum embedded ribosomes synthesize proteins, also modify proteins and produce membranes smooth endoplasmic reticulum contains embedded emzymes which catalyze synthesis of carbohydrates and lipids, detoxification of foreign substances golgi apparatus recieve and process materials from the rough endoplasmic reticulum and send to other areas of the cell lysosomes degrading enzymes which catalyze the rapid breakdown of proteins, nucleic acids, lipids and carbohydates peroxisomes involved in the oxidation of fatty acids vacuoles organelles in plant cells which help cell maintain osmotic balance mitochondria organelles which contain their own DNA and contain the proteins which carry out oxidative metabolism providing energy to the cell chloroplasts found in plant and some bacterial cells, manufacture their own food through photosynthesis components of the cytoskeleton actin filaments (cellular movement), microtubules (intracellular movement of materials), intermediate filaments (structural support) monomers of proteins amino acids monomers of nucleic acids nucleotides monomers of polysaccarides monosaccarides monomers of lipids fatty acids dehydration synthesis how macromolecules are synthesized, water released hydrolysis how macromolecules are broken down, water needed major uses of carbohydrates energy sources, structural roles, identfication isomers same chemical formula but different structures glycosidic linkage covalent bond between monosaccarides number 1 carbon carbon farthest to the right, then number clockwise cellulose unbranched polymer of glucose, beta 14 glycosidic linkages, found in cell walls starch branched polymers of glucose, alpha 14 linkages with alpha 16 branches, used in plants to store glucose for later energy needs glycogen extra branched polymers of glucose, alpha 14 linkages with alpha 16 branches, used in animals to store glucose for energy needs alpha/beta glucose hydrogen above/below molecule major uses of proteins enzyme catalysis, defense, transport, support, motion, regulation, storage composition of an amino acid amino acid group (NH2) and carboxyl group (COOH) bonded to carbon along with functional side group type of bond in protein peptide bond four classes of amino acid R groups uncharged polar, uncharged nonpolar, acidic, basic hydrophobic water fearing (nonpolar R groups) hydrophyllic water loving irreversible enzyme inhibitor permanently bind to or modify active site, render enzyme unusable competitive reversible inhibitor physically resembles substrate, bind to active site to prevent enzyme activity but can be knocked out without harming enzyme noncompetitive reversible inhibitor bind to enzyme somewhere other than active site, indirectly prevent substrate from binding, can become unbound without harming enzyme primary structure amino acid sequence secondary structure interaction of groups in the peptide backbone, alpha helices or beta pleated sheets tertiary structure interactions between amino acid side groups quarternary structure interactions between two or more polypeptide subunits chaperone proteins help other proteins to refold correctly initially or after becoming denatured denaturation causing proteins to unfold and lose function by changing the pH, temperature or ionic concentration of solution two types of nucleic acids DNA and RNA pyrimidines uracil, cytosine, thymine purines adenine, guanine how DNA and RNA differ which nucleotide bases and sugars it contains composition of a nucleotide five carbon sugar with 5' phosphate group, 3' hydroxyl group and nitrogenous base ATP nucleotide with 3 phosphate groups which can be broken off to provide energy for cellular activities triglyceride three fatty acids bonded by ester linkages to glycerol backbone phospholipid glycerol, 2 fatty acids and phosphate group. polar head and nonpolar tail allows for formation of membranes phosphatidl gylcerol based lipid sphingomyelin only phospholipid that is not glycerol based (serine based) saturated fat fatty acid 'saturated' with hydrogens, no kinks in tail, solid at room temperature unsaturated fat contains carboncarbon double bonds, causes kinks in tail, liquid at room temperature glycolipids membrane lipid with sugar attached used for cellular identification on extracellular leaflet Cell Theory 1) All organisms are composed of one or more cells, and the life processes of metabolism and heredity occur within these cells 2)Cells are the smallest living things, the basic units of organization of all organisms 3) All cells come from preexisting, living cells The reasons why cells are small; the rate of diffusion is affected by: 1) surface area available for diffusion 2) temperature 3) concentration gradient of diffusing substance 4) distance over which diffusion must occur Define resolution The minimum distance two points can be apart and still be distinguished as two separate points Human resolution limit is: Light microscope is: Electron microscope is: 100um 200nm 0.2nm Vertical Gene Transfer (VGT) Genes are passed from generation to generation Horizontal Gene Transfer (HGT) Hitchhiking genes from other species gene transfer between different species. Most prevalent in very early in the history of life, when the boundaries between individual cells and species seem to have been less firm than they are now and DNA more readily moved among different organisms Why was rRNA used to determine differences between the 3 domains? 1) Evolutionarily ancient 2) Found in all organisms 3) Same function in all organisms (all organisms make protein, and use rRNA to make protein) 4) Highly conserved (it hasn't changed much), so any change is significant Methanogens Obtain their energy by using hydrogen gas (H2) to reduce carbon dioxide (CO2) to methane gas (CH4) Strict anaerobes oxygen is very toxic to them Live in swamps, marshes, intestines of mammals Extremophiles Able to grow under extreme conditions: Temperature (cold and hot), salty environments, pH tolerant, pressure tolerant Nonextreme archaea Grow in the same environment that bacteria do Endosymbiosis Theory that proposes that eukaryotic cells evolved from a symbiosis between different species of prokaryotes. Mitochondria and chloroplasts The 3 characteristics that separate eukaryotes from prokaryotes: 1) Multicellularity 2) Compartmentalization 3) Sexual reproduction Dehydration reaction (condensation) The removal of an OH from one monomer and H from the other monomer to link them together. This reaction takes place the same for EVERY macromolecule group. Hydrolysis When cells disassemble macromolecules into their constituent subunits through reactions that are the reverse of dehydration a molecule of water is added instead of removed A hydrogen atom is added to one subunit and a hydroxyl group is added to the other, breaking a specific covalent bond in the macromolecule Functions of the nucleus (3) 1) Keeping & replicating the DNA 2) Distributing out genetic information through RNA (mRNA to be specific) through TRANSCRIPTION 3) The NUCLEOLUS in the nucleus assembles and produces ribosomal subunits (once exported out will continue to carry out protein synthesis) Functions of the rough endoplasmic reticulum (3) 1) Secretion & processing of proteins (protein modification) 2) Start process of inserting proteins into membrane of rough ER 3) Can form vesicles to be transferred to other locations Functions of the smooth endoplasmic reticulum 1) Detoxication of cytoplasm so that substances cannot be dangerous to the cell anymore (liver cells have a lot of SERs) 2) Synthesis of lipids 3) Stores Ca 3+ in cells keeps cytoplasmic level low Polyribosome collection of ribosomes working together making the same protein (multiple copies) They don't necessarily work TOGETHER, they just happen to be in the same place at the same time working on synthesizing the same copies of the same protein. They DO NOT influence each other. Function of mitochondrian Produces ATP for the cell major contributor of ATP to the cell Functions of the Golgi body (2) 1) "Post office" of the cell. It recognizes where that specific protein sent from the ER is supposed to go and sends it there 2) Continues the modification of proteins sent from the ER Composition of macromolecules in the "dry weight" of the cell Proteins (>1/2 of the weight) > Nucleic acids > Carbohydrates > Lipids Macromolecules and their monomers Proteins > Amino acids Nucleic acids > Nucleotides Polysaccharides > Monosaccharides Lipids > Fatty acids Functions of carbohdrates (4) 1) Energy sources breaking it down to obtain ATP 2) A plant's cell wall 3) Cytoskeleton in insects, crustaceans, etc. 4) Cell surface recognition markers Homodimer Two subunits that are identical to each other Heterodimer Two different subunits How are disulfide covalent bonds made? 2 cysteines that somehow find each other in 3D space, and also the enzyme that helps this covalent bond to form Denaturing Removal or inactivation of stabilizing forces to unfold the protein down to its primary structure This does NOT mean that the protein is destroyed, rather just reduced to its primary structure. (Breaking hydrogen, ionic, covalent bonds etc.) Chaperones The group of proteins that prevent inappropriate interactions within proteins Biosynthetic / Anabolic Reactions Linking together of smaller molecules to larger molecules (i.e. dehydration / condensation reaction) Require a significant amount of energy to proceed endergonic Catabolic Reactions Break down larger molecules into smaller molecules (i.e. hydrolysis reactions) Releasing of energy Referred to as spontaneous exergonic Allosteric site A site other than the active site where reversible, noncompetitive inhibitors bind to. Binding here will change the shape of the enzyme, therefore not allowing substrates to bind to it. Purines Two rings in its structure. Adenine and Guanine Pyrimidines One ring in its structure. Cytosine, Thymine, and Uracil "Tidyl" Backbone provided by glycerol Amphitatic A molecule that has both a hydrophillic as well as a hydrophoic region on it Transmembrane proteins Proteins that go THROUGH the phospholipid bilayer Integral proteins Proteins that are attached to one leaflet of the phospholipid bilayer Lipid linked proteins Proteins that are linked to the bilayer by lipids in the bilayer Protein attached (peripheral proteins) Proteins that are attached to the bilayer through hydrogen bonds, ionic bonds, basically bonds that can be broken without disturbing the integrity of the phospholipid bilayer
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