Study Guide for Midterm 1
Study Guide for Midterm 1 ZOOLOGY 151
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This 4 page Study Guide was uploaded by Sarah Arndt on Thursday February 18, 2016. The Study Guide belongs to ZOOLOGY 151 at University of Wisconsin - Madison taught by Seth Blair in Winter 2016. Since its upload, it has received 91 views. For similar materials see Introduction to Biology in Animal Science and Zoology at University of Wisconsin - Madison.
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Date Created: 02/18/16
Study Guide midterm #1 Bio 151 Cell theory 1. All living organisms are made of cells (and the products of cells) 2. All cells are produced by other cells. 3. The cell is the basic unit of structure Natural Selection 1. There is a variation of traits within the population of individuals that make up a species. 2. Those traits are inheritable. 3. Certain traits allow better survival of individuals Water properties Binds to charged or polarized molecules and surfaces: adhesion Cohesion: water binds to water Ice is less dense than liquid water High specific heat Prokaryotic Cells Bacteria and archaea DNA, cell membrane, cell wall, cytoplasm Eukaryotic Cells Membranebound organelles in cytoplasm, DNA in nucleus Hydrocarbon Only carbon and hydrogen in chains and rings Hydrophobic Nonpolar, doesn’t like water Hydrophilic Polar, likes water Reactants Anabolic: chemical reaction builds larger, more complex molecule Catabolic: chemical reaction breaks down molecule into simpler, smaller molecules Energy in Bonds Laws of thermodynamics 1. Total energy in system is constant, can’t be created nor destroyed 2. An increase in the sum of entropies in the participating system Kinetic energy: energy of motion Potential energy: stored ability to cause motion Break bond: released potential energy becomes kinetic, molecular motion=heat, or make another chemical bond Spontaneous: temporary release of energy, changes in entropy=changes in Gibbs free Energy = Change in G, release free energy, negative=exergonic Nonspontaneous: absorbs free energy, positive=endergonic Enzymes Catalysts: speed up reactions by lowering activation energy First discovered was diatase: speeds starch into sugar Lock and key interactions: binding between molecules, usually temporary, based on many noncovalent bonds Macromolecules Four, 3 of 4 are polymers Polymer: chain of similar monomer subunits Carbohydrates Add many hydroxyl groups and one carbonyl group to short hydrocarbon chains Named: ose Functions: energy, enzymes, structure Joined by glycosidic linkages Polysaccharides: store energy, make support structures like cellulose and chitin Proteins Amino group, carboxylic acid, r group Peptide bonds link them together Primary structure: order of amino acids in polymer Secondary: fold into alpha helix or beta pleated sheet Tertiary: all other types of folding (covalent, disulfide, ionic, hbonds, vander walls, and hydrophobic interactions) Quaternary: created by nonpeptide bonds between separate amino acid polymers Denaturation: loss of 2 , 3 , and 4 structure Functions: enzymes, structure, pumps, and switches Lipids Membranes define cell boundaries Store and release energy, help with signaling between cells Contain hydrophobic hydrocarbon chains Phospholipids: polar head, nonpolar tails Diffusion Molecules going across parts of the cell Passive: no energy needed Active: energy needed such as atp Permeability of Lipid Bilayer Permeable to large and small non polar molecules (O2 and N2) and Small polar molecules Impermeable to large polar molecules like glucose and sucrose Concentrations Isotonic: concentration is the same outside and inside the cell, like sea water Hypotonic: low outside cell, like fresh water Hypertonic: high outside, like evaporate sea water Membrane Vesicles Small membranebound compartments inside cells Trans Membrane Proteins Embedded in membrane, spans width of lipid bilayer Facilitated diffusion High to low Through channels or carrier proteins Active Transport Against concentration gradient Cotransport: diffusion of one molecule drives active transport of second Uses ATP Nucleic Acids Nucleotide monomer that contains a nitrogen base, phosphates, and a monosaccharide DNA: ACGT o Double helix, hbonding between nucleotides o 1 purine and 1 pyrimidine to get the correct width o two strands run in opposite directions Replication one strand is template for making new complementary strand separate, add matching nucleotides, ligate semiconservative model: one new, one mix conservative: one new, one old dispersive: both mixtures 1. Helicase separates and binding proteins stabilize 2. DNA polymerase makes new nucleotides, Origin of replication: place where replication starts, makes replication bubble Process runs along in both directions Problems o Unwinding a helix creates supercoiling so topoisomerase cuts strands ahead o DNA polymerase can only add bases to extant DNA or RNA strand so it makes an RNA primer o Only works in one direction so has to keep restarting creating Okazaki fragments o Telomerase is used in germ line, stem, and cancer cells so the ends don’t keep getting shorter Ribosomes Catalyze protein synthesis, outside nucleus in cytoplasm RNA types Ribosomal RNA writes protein codes Messenger RNA transfers code from DNA to Ribosome Transcription: of RNA from DNA template Requires RNA polymerase Only single strand made Promoter DNA: where RNA polymerase binds and transcription starts Terminator DNA: where transcription ends Transcription units: regions of DNA transcribed into mRNA Factors: used by most genes to help RNA polymerase, recognize and bind to promoter nucleotides, one in bacteria, several in eukaryotes Ribosome moves from 53 on mRNA=proteins Adaptors: transfer RNA: small, stable, 7080 nucleotides, each type of tRNA binds a specific type of amino acid Aminoacul tRNA synthetases How tRNA gets its amino acid Different ones for each type Specific ones use ATP energy to attach specific amino acids to specific tRNA The roles of RNA in translation 1. rRNA: with proteins make the ribosome which is the machine for making proteins 2. mRNA: codons translated into protein at ribosome 3. tRNA: brings amino acid to ribosome, each tRNA carries a specific amino acid Starting/Stopping 1 start codon: AUG 3 stop codons: UAA, UAG, UGA
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