Bio 150, 2/12-2/19
Bio 150, 2/12-2/19 Biology 150
Popular in introduction to biological sciences
Popular in Biology
This 5 page Class Notes was uploaded by Matthew Hubecky on Thursday March 3, 2016. The Class Notes belongs to Biology 150 at Southern Illinois University Edwardsville taught by Dr. Theodorakis in Spring 2016. Since its upload, it has received 20 views. For similar materials see introduction to biological sciences in Biology at Southern Illinois University Edwardsville.
Reviews for Bio 150, 2/12-2/19
Report this Material
What is Karma?
Karma is the currency of StudySoup.
Date Created: 03/03/16
1. Cilia & flagellamovement and located on the exterior of the cell Cilia are short and numerous; they beat back and forth like an oar Functions of cilia movement for some protists, food capture in filter feeders, and to move fluids or ova in multicellular organisms Flagella long, one or two per cell, move side to side like a whip Ex: some protists have flagellum, sperm cells for example Structure of cilia and flagella—microtubules, composed of 9 doublets (pair of microtubules) around the outside and two in the center (9=2 arrangement) motor proteins on doublets “walk” up and down neighboring doublets doublets slide past each other B. Animal vs. plant vs. fungal cells Cell wall Chloroplasts Central vacuole Animals No No No Plants Cellulose Yes Yes Fungi Chitin No No All other organelles are the same II. Prokaryotic cells A. External features cell wallpeptidoglycan Flagellumspins instead of whipping. Pulls instead of pushing the cell Pillishort projections Functions: exchange of DNA sequences (plasmids), attachment in some bacteria, and movement in some bacteria as a “crawling” mechanism B. Internal features Nucleoidregion where single circular chromosome (DNA) is at, no membrane on nucleoid Plasmidssmaller circular exchromosomal DNA. Can be copied and exchanged between cells. Antibiotic resistance genes are found on plasmids Photosynthetic species have membranous flat sacs where photosynthesis occurs, the only membranous organelles most species of bacteria have a cytoskeleton for support and all have ribosomes C. Prokaryotes vs. Eukaryotes Prokaryotes Eukaryotes Cell wall Peptidoglycan Cellulose or chitin True nucleus No Yes Mitochondria No yes Membranous organelles No* yes *Except for photosynthetic membranes Enzymes I. Nature of enzymes most are proteins a few are made of RNA (ribozymes in some protists) Catalyze chemical reactions II. Chemical reactions exergonic reactionreleases energy and happens spontaneously exergonic products have less energy than the reactants Endergonic reactionrequires/ absorbs energy endergonic reactions do not happen spontaneously endergonic products have more energy than reactants *in living things, energy comes from ATP III. Enzymecatalyzed reactions A. Substrate & products substrate→products The transition state is the intermediate between substrate and products. B. Mechanisms of action bring substrates into close proximity bind substrates in “active site” might strain chemicals which makes them easier to break might provide a favorable chemical environment might donate or accept electrons C. Types of enzymecatalyzed reactions 1. Catabolic reactions (catabolism) large molecule is broken down into two or more smaller molecules releases energy 2. Anabolic reactions (anabolism) small molecules are converted to large molecules requires energy and uses ATP ex: amino acids convert to a protein, nucleic acids convert to DNA or RNA 3. Isomerization reactionconvert between isomers ex: glucose to fructose, both are C6H12O6 4. Phosphorylationadd phosphate (PO4), requires ATP Dephosphorylation is the opposite, it removes a PO4 5. Oxidation/Reduction (redox) Oxidation removes e and H+ Reduction adds e and H+ redox reactions usually occur together. They oxidize one substrate and reduce another substrate IV. Nature of enzymes A. Saturation kinetics slope = km = affinity of enzyme for substrate B. “Helper” moleculessome enzymes need cofactors non Protein molecules that noncovalently bind to the enzyme they are required for enzyme activity can be inorganic (ex: metal ion Cu+2 or Fe+2) can be organic, called a coenzyme C. Specificity of enzymeseach enzyme catalyzes one reaction D. Enzymes not affected by reaction (usually) temporarily change shape (conformation) during the reaction temporarily change molecular structure of amino acid side chains both are reversible changes E. Nomenclature (Substrate name or type of reaction) + ASE = name Ex: phosphorylaseremoves PO4 Isomerase isomerizes molecule Protease breaks down proteins V. Factors that affect enzyme function A. Physical conditionsex: Ph/Temperature influences reaction rate optimum (Ph, temp.) B. Regulation of enzymes 1. Backgroundactivity can be increased or decreased by certain chemicals 2. Noncovalent modificationbinding of chemicals a. Inhibition within active site (competitive inhibition) prevents substrate binding at a site on enzyme other than active site is called allosteric inhibitor *can have allosteric activation too 3. Covalent modification Ex: phosphorylation or Dephosphorylation, either may activate or deactivate and enzyme VI. Biochemical pathways A. Definitionchain of chemical reaction where the product of one enzyme is the substrate of the next enzyme B. Feedback loopsproducts of “downstream” reaction can inhibit or stimulate “upstream” reaction Ex: intermediate 2 inhibits enzyme 1. It controls the rate of the reaction. Cellular Respiration – how ATP is made I. Aerobic Respiration A. Background 1. Overall question: how do cells use sugar and oxygen to make ATP? 2. Overview of aerobic respiration a. Overall formula Glucose + NAD+ O2+ ADP+ PO4→CO2+ H20+ATP+NADH This is an oxidation reaction multiple steps are used to oxidize glucose in order to more efficiently capture energy b. Steps4 main steps Glycolysis, preparation for Krebs cycle, Krebs cycle, and electron transport chain 3. Electron carriersorganic molecules that accept/donate electrons during redox reactions, electrons are given to electron carriers there are 2 types of electron carriers a. NAD+ +2e +2H+→NADH + H+ Made from riboadenosine and niacin b. FAD +2e +2H+→FADH2 Made from adenosine and riboflavin 4. ATP ATP→ADP + PO4 ↓ Energyused for movement (motor proteins), active transport, anabolism 5. Review of mitochondrial structure Outer mitochondrial membrane (omm) Intermembrane space (ims) Inner mitochondrial membrane (imm) Matrix B. Glycolysis 1. Overall equation Glucose+2ATP +4ADP+2PO4+2NAD+→ 2Pyruvate + 2ADP + 4ATP + 2NADH (+H+) Uses 2ATP to gain 4ATP, so the net gain is 2ATP 2. Location in cellcytoplasm (cytosol) 3. Phases a. Energy investment phase b. Cleavage phase c. Energy liberation phase 4. Net Output C. Preparation for Kreb’s cycle 1. Overall equation 2. Location in cell 3. Net output D. Kreb’s cycle 1. Overall equation 2. Location in cell 3. Steps 4. Net output E. Overall purpose of glycolysis & Kreb’s cycle F. Electron transport chain 1. Definition & location 2. ETC w/ NADH 3. ETC with FADH 2 4. ATP synthesis 5. Output G. Relative output of ATP H. Regulation of glycolysis and Kreb’s cycle I. Other macromolecules II. Anaerobic fermentation A. Definition B. Overall reaction C. Purpose D. Output