BioExam1StudyGuide.pdf BIOL 160 - 018
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BIOL 160 - 018
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This 15 page Study Guide was uploaded by Caroline Emery on Friday September 11, 2015. The Study Guide belongs to BIOL 160 - 018 at University of Tennessee - Knoxville taught by John W Koontz in Fall 2015. Since its upload, it has received 669 views. For similar materials see Cellular and Molecular Biology in Biology at University of Tennessee - Knoxville.
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Date Created: 09/11/15
Through Exam 1 911 Chapter 2 Water and Carbon Molecules Formed when atoms bond to each other Water is most important to life Molecular weight is sum of mass of all the atoms in the molecule One mole 6022 x1023 molecules has mass equal to molecular weight in grams Concentration in molarity molesliter Water Most important for life Highly polar forms hydrogen bonds 0 Oxygen is more electronegative than hydrogen 0 H gets partial charge o 0 gets partial charge Polar molecules readily dissolve in water nonpolar molecules do not Cohesion binding between water molecules 0 Leads to surface tension Adhesion bonding between unlike molecules Crystal lattice in solid form allows ice to oat and allows life Large capacity to absorb heat 0 High speci c heat and high heat of vaporization Bonds 0 Number per atom depends on valence Covalent o Nonpolar electrons are evenly shared and bond is symmetrical 0 Polar covalent symmetrically shared Electrostatic ionic o Electrons transferred to one atom from another Hydrogen 0 Weak electrical attractions between H and an electronegative atom with a partial charge Van Der Waals Hydrophobic Atoms Protons positive charge 1 amu in nucleus gives atomic number Neutrons no charge 1 amu in nucleus combines with Protons for atomic weight Electrons negative charge in orbitals Orbitals Electrons move in speci c patterns around the nuclei Grouped into levels called orbitals Outermost orbital are valence electrons Unpaired valence electrons are available for bonding Reactions When a substance is formed or is broken down Have products and reactants Chemical equilibrium is when the forward and reverse reactions happen at the same rate and the ratio of products to reactants stays constant Spontaneous if they lead to lower potential energy and higher entropy Nonspontaneous if energy is input Endothermic reactions need heat to continue exothermic reactions produce heat pH Based on proton H concentration pH of water is 7 neutral Acids have pH less than 7 Bases have pH more than 7 In acidbase reactions a proton donor acid transfers a proton to a proton accepter base Buffers compounds that minimize changes in pH Energy Capacity to do work or supply heat Potential energy stored energy energy of position 0 Electrons in outer shells have more PE than internal electrons Kinetic energy thermal energy temperature heat it thermal energy transferred between two objects of different temps First Law of Thermodynamics energy is conserved not created or destroyed only changed Entropy S amount of disorder in a group of molecules Second Law of Thermodynamics entropy always increases Gibbs Equation AG determines spontaneity o AGAH TAS H potential energy enthalpy S entropy disorder becomes more important as temp increases 0 AG gt O is exergonic spontaneous 0 AG lt O endergonic and requires energy input 0 AG reaction at equilibrium Chemical Energy Potential energy stored in chemical bonds Solar energy is converted into chemical energy by photosynthesis 9 caloriesgram for fats and 4 caloriesgram for carbohydrates Carbon most versatile atom on Earth four valence electrons can form many covalent bonds Functional Groups Amino group attract a proton acts as a base amines o Nitrogen bonded to two H Carboxyl groups drop a proton Carboxylic acids 0 C single bonded to OH and double bonded to O Carbonyl groups sites of reactions that link molecules into larger compounds aldehyde outside or keytone internal 0 CO Hydroxyl groups weak acids alcohols o COH Phosphate groups two negative charges organic phosphates o P single bonded to three 0 two negative charged one attatched elsewhere and double bonded to one 0 Sulfhydryl groups link together via disul de groups Thiols 0 SH Chapter 3 Proteins Proteins Cell functions depend on them Made of amino acids In cells many are enzymes that act as catalysts Structure Primary amino acid sequence Secondary alpha helices and beta sheets Tertiary interactions between amino acids that dictate a protein s shape Quaternary Interactions between polypeptides to form one protein Denatured unfolded proteins can t function Molecular chaperone proteins help proteins fold correctly Prions are improperly folded normal proteins Amino Acids Only 20 All have a central atom bonded to NH2 COOH H and an 39R group 0 R group causes all amino acid variation 0 Hydrophobic nonpolar R groups no hydrogen bonds 0 Hydrophilic polar R groups hydrogen bonds dissolve in water Polar charged Polar uncharged acids are negative bases positive 0 R groups with hydroxyl amino carboxyl or sulfyhydral groups are more reactive than hydrocarbon side chains In the ionized form the amine group takes an extra H and the carboxyl loses an H Monomers and Polymers midsized molecules amino acids or nucleotides are in small monomers link together polymerize to form polymers Macromolecules are large polymers made of many Polymerization is non spontaneous Monomers polymerize through dehydration synthesis condensation reactions where water is released 0 Hydrolysis is the opposite polymers broken down by adding water 0 Amino terminus is the end amino group and the c terminus is the end carboxyl group Peptide Bonds Condensation reactions bond the carboxyl group of an amino acid to the amino group of another to form a peptide bond 0 Chain of amino acids liked by peptide bonds is a polypeptide 0 Less than 50 amino acids are oligopeptides o More than 50 are called proteins Functions Catalysis enzymes speed up reactions 0 Most fundamental of functions 0 Bring substrates together correctly 0 Decreases kinetic energy needed for reactions lowers EA by lowering the free energy of the transition state 0 Do not change AG and aren t consumed in the reaction 0 Reaction speci c 0 Steps of Enzyme Catalysis 1 lnitiation substrates are oriented correctly 2 Transition State Facilitation substrate and R group interactions lower activation energy 3 Termination reaction products are released Defense antibodies Movement motor and contractile proteins Signaling convey signals between cells Structure de ne shape and body structures Transport transport proteins carry materials membrane proteins carry things in and out of the cell Chapter 4 Nucleic Acids Nucleotides Contain a sugar a phosphate group and a nitrogenous base Ribo form RNA Deoxyribo form DNA Nucleic acids form when nucleotides polymerize Phosphodiester linkagebond form between the phosphate on the 539 C of one nucleotide and the OH on the 339 C of another 0 Always written 5 l 3 Polymerization is endergonic and uses enzymes 0 Energy comes from the phosphorylation transfer of phosphate groups to a substrate of nucleotides Nucleoside triphosphates are reactants in polymerization DNA 0 Primary structure sequences of nitrogenous bases secondary is a double helix with parallel and opposite base pairing Allows organisms to store and replicate info needed to survnve Deoxyribonucleotides Watson and Crick Antiparallel con guration Double helix Bases on the inside Purines A and G pair with Pyrimidines C and T 00000 A T has two hydrogen bonds 0 CG has three hydrogen bonds Replication o Complimentary base pairing means each strand is a template for its compliment 0 Steps 1 Separation of double helix 2 Hydrogen bonds between deoxyribonucleotides with complimentary bases on original template strand and phosphodiester bonds forming the new complimentary strand 0 Stability makes DNA a poor catalyst RNA 0 Primary structure is sequence of nitrogenous bases secondary is short double helices and hairpins Likely the rst self replicating molecule Ribonucleotides First lifeforms probably made of RNA 0 One more OH group than DNA makes it more reactive and less stable Uracil instead of Thymine Intermediate between DNA and proteins 0 Can be informationcontaining and can selfreplicate Can be catalytic o Ribozymes are enzymelike RNA Temperature and Reactions 0 Rate of reactions depends on number of collisions and increased templjl more collisionsfaster reaction Chapter 5 Carbohydrates Monosaccharides Simple sugars that vary in four ways 1 Location of the carbonyl group a Aldose end of the monosaccharides b Keytose middle of the monosaccharides 2 Number of carbons a3tnose 10 b 5 pentose c 5 hexose 3 Spatial arrangement of hydroxyl groups 4 Linear or rings Polysaccharides Complex Carbohydrates Polymers of monosaccharide monomers Simplest ones are disaccharides made of two monosaccharides Simple sugars form from condensation between hydroxyl groups causes glycosidic linkage 0 Alpha is when OH groups are on the same sides 0 Beta when not on the same side Common Carbohydrates Glycogen and Starch energy storage animals plants 0 Hydrolysis of alpha linkages in glycogen catalyzed by phosphorylase Contained by most cells to provide glucose 0 Alpha linkages in starch are hydrolyzed by amylase Key role in carb digestion Chitin and Cellulose structure animals plants Peptidoglycan cell structure Function 0 Cell identity 0 Glycoproteins are proteins covalently bonded to carbs 11 Key in cellcell recognition and signaling 0 Store energy 0 Undergo reactions to form adenosine triphosphate ATP Free energy in ATP is used for endergonic reactions Carbs have a lot of CH bonds so they have a lot of free energy 0 Fatty acids have even more Fibrous structure Precursors to larger molecules Chapter 6 Lipids and Membranes Lipids Mostly nonpolar and hydrophobic Hydrocarbons are nonpolar and only contain C and H 0 Don t dissolve in water due to fatty acids 0 Hydrocarbon chain bonded to a carboxyl Fatty acids and isoprene are primary components 0 3 Types 1 Triglycerides energy storage a 3 fatty acids ester linked to a glycerol b formed by dehydration synthesis 2 Phospholipids membranes a Amphipathic 12 i quotheadquot hydrophilic glycerol phosphate and charged groups highly polar covalent quottaiquot two nonpolar fatty acid or isoprene chains b Allows membranes to form with heads outside and tails inside c Do not dissolve in water d In water spontaneously forms either i Micelles heads face water tails face each other ii Phospholipid bilayers 1 Selectively permeable small or nonpolar molecules affected by number of double bonds length of tail amount of cholesterol decreases permeability temperature Fluidity individual phospholipids can move laterally almost never ip across membrane 3 Steroids Cholesterol membranes and metabolic intermediates Solute Movement 13 Passive transport no energy is added Active transport energy is needed Diffusion random movement of solutes 0 Concentration gradient spontaneous Equilibrium once molecules are randomly dispersed through the solution still movement but no net movement Osmosis movement of water to create equal concentrations 0 Moves from low solute concentrations to high 0 Only occurs across a selectively permeable membrane Fluid Mosaic Membrane Model 0 Proteins are inserted into the lipid bilayer Makes bilayer uid dynamic mosaic of phospholipids and proteins lntegral proteins amphipathic so it can span the entire membrane 0 Transmembrane span entire membrane Transport proteins 1 Channels passive a lon channels allow ions to flow across the membrane down their electrochemical gradient b Facilitated passive diffusion by channels that allows molecules that couldn t pass otherwise 2 Carrier proteins transporters passive a Change shape during process b Down concentration gradient c Used to move glucose 3 Pumps active a Move ions or molecules AGAINST the gradient b Sodiumpotassium pump 14 15 c Make cotransport possible 0 Peripheral one side of the membrane
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