Exam 1 Study Guide
Exam 1 Study Guide Bio201
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This 5 page Study Guide was uploaded by Justin Abeles on Saturday February 14, 2015. The Study Guide belongs to Bio201 at University at Buffalo taught by Dr. Laura Hudson in Spring2015. Since its upload, it has received 1521 views. For similar materials see Cell Biology in Biology at University at Buffalo.
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Yes YES!! Thank you for these. I'm such a bad notetaker :/ will definitely be looking forward to these
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Date Created: 02/14/15
Relativ e Streng th Biology 201 Exam 1 Study Guide Justin Abeles Important Biological Groups Hydroxyl Alcohols Carbonyl AldehydesKetones Carboxyl Carboxylic Acids Amino Amines Sufihydral Thiol Electronegativity Tendency to attract electrons Small differences lead to charge asymmetry I Dipoles Bond Types Covalent Bonds 0 Like to exist in pairs 0 Unpaired electrons are unstable and like to pair With unpaired electrons from other atoms Ionic Bonds 0 Ionization of molecules into cations and anions 0 Charge attraction I Ionic Bonds Hydrogen Bonds 0 Polar molecules attract are held together by hydrogen bonds 0 Polar molecules are stabilized by interactions With water 0 Hydrophilic Van der Waals O Nonpolar molecules form transient dipoles may interact stabilized O Hydrophobic 0 Individual very weak Together very strong pH Scale of 114 17 are acids 714 are bases 7 is neutral pH log Molarity I Expressed power of Molarity is the pH XIOA7 7pH O Buffer Minimizes changes in pH I Water is a terrible buffer OOOOO Biological Macromolecules 0 Proteins functionenzymes signaling structure 0 Amino Acids 0 Nucleic Acids Information storage functionribozymes O Nucleotides 0 Polysaccharides Energy storage structure 0 Monosaccharides 0 Lipids Compartmentalization energy storage signaling 0 No polymers Polymerization of Biological Macromolecules 0 Condensation and release of H20 0 Requires energy Depolymerization of Biological Macromolecules 0 Hydrolysis Reaction 0 Consumes H20 0 Release Energy Amino Acids 0 Chiral 0 Left or right handed 0 All left except for glycine 0 Distinctions 0 Non polar Hydrophobic All C s and H s 0 Polar uncharged OH or NH2 and CO 0 Polar charged NHX or COOH 0 Special Cases 0 Cysteine Disulfide bonds 0 Glycine Non polar nonchiral O Proline Forms rings in oxidizing environment resists exibility Proteins 0 Amino Acids added onto carboxy terminus to increase size 0 Levels of structure 0 Primary 1 Linear arrangement of amino acids 0 O O O Fibrous and globular proteins Secondary 2 ahelices and bsheets hydrogen and ionic bonds Tertiary 3 3D structure covalent ionic hydrogen and van der waals bonds Quaternary 4 multisubunit proteins homoheteromultimers Protein Folding Polysaccharides Lipids 0 Changed amino acid in sequence I change in shape I change in protein function 0 Can cause disease ex Sickle cell anemia 0 Sugars O Polysaccharides Energy storage and structure 0 Monosaccharides CXH20y 0 Polymerization of sugar I glycosidic linkage I Glucose Polymers O Cellulose Structural B1 4 Glycosidic linkages animals can t digest O Glycogen Energy storage Al 4 Glycosidic linkages animals can digest 0 Lipids 0 Fatty Acids I Secondary energy source I RCOOH R is CH2X I C 1224 Transfats Derived from chemical hydrogenation of cis fatty acids Triglycerides Great energy storage molecule Phospholipids important amphipathic molecules Steroids complex diverse function FOUR FUSED RINGS Saturation More saturated more H s higher Tm I Unsaturated At least one cc double bond bent and rigid I Saturated ACC bonds straight but exible OOOOO Phospholipids and Nucleic Acids 0 Phospholipids 0 Polar molecule phosphate and glycerol backbone Hydrophilic head 0 Fatty acid chainsHydrocarbon chains Hydrophobic tail 0 Nucleic Acids O Polymerize 5 I 3 0 DNA Deoxynucleic Acid 0 RNA Ribonucleic Acid 0 Structure I Base Acid Nucleoside Phosphate I Base Pyrimidines or Purines One or two hexagons 0 Differences I H vs OH on 2 Carbon I Deoxygenation of 2 OH requires an extra enzymatic reaction I 2 H makes DNA backbone more stable Types of RNA 0 Messenger RNA mRNA Intermediate that gets translated to protein 0 Transfer RNA tRNA Brings amino acids to growing polypeptides 0 Ribosomal RNA rRNA Part of ribosome catalyzes polymerization of polypeptides Cells 0 Prokaryotes 0 Plasma membrane and cell wall 0 No membrane organelles O Classified as a gramnegative or a grampositive 0 Small typically 12 um I Eukaryotes 0 Loss of peptidoglycan cell wall 0 Gain of cytoskeleton O Membranebound organelles 0 Increased cell size 0 Endosymbiosis O Anaerobic eukaryote ingests aerobic bacteria 0 DiVide intracellularly 0 Loss of essential function I Bacteria can t survive outside I Centrifugation O Separates organelles based on masses I Organelles O Nucleus I Contains chromosomes I Location of RNA transcription I Contains Nucleolus which transcribes RNA and assembles ribosomes 0 Endomembrane System I Rough ER w ribosomes protein synthesis core glycosylation I Smooth ER no ribosomes glycogen breakdown lipid synthesis Ca storage I Golgi Complex Protein glycosylation and sorting I Vesicles transport I Lysosomes Digestion and breakdown O Golgi Complex I Not interconnected with ER I Located near centrosome I Cis medial and trans Differences in RNA Transcription 0 Eukaryotes I Multiple RNA s transcribed simultaneously I Translation after mRNA leaves nucleus I Lag between transcription and translation I Quality control and mRNA processing 0 Prokaryotes I Occurs in cellulose I Simultaneous transcription and translation I Fast I No time for quality control 0 Pulse Chase Experiment 0 How secreted proteins are made and transferred 0 Types of Secretion I Regulated Requires a stimulus I Constitutive Constant I Ca role in cell membranes
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