Biology Exam 1 Study Guide
Biology Exam 1 Study Guide BS 161
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This 13 page Study Guide was uploaded by Sarah Struble on Friday October 2, 2015. The Study Guide belongs to BS 161 at Michigan State University taught by D. Koslowsky, J. Merrill in Fall 2015. Since its upload, it has received 500 views. For similar materials see Cell and Molecular Biology in Biology at Michigan State University.
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Date Created: 10/02/15
fof13 BS 161 Exam 1 Study Guide Ch 1 through 5 Electrons key to chemical behavior of atoms valence electrons electrons in outer shellorbital orbital area around the nucleus where an electron is most likely to be found each orbital holds two electrons first energy level one orbital s orbital holds 2 electrons second energy level one sorbital three porbitals holds 8 electrons electrons farther from nucleus have higher potential energy Octet Rule atoms want full energy levels full energy level 8 electrons atoms fill their outer shells by covalent bonds so that they can have 8 valence electrons gtC needs one more e to have full energy level CI If f 939quot 1 Cl 1quot gtUses H s one e to fill the energy level 39 g Electronegativity attraction of electrons to atoms electronegative atoms hold their electrons and the electrons in bonds closer to them a very electronegative atom bonded to a less electronegative atom a polar covalent bond Br has a partial negative H has a partial posmve charge Charge because it is because Br 393 pUH39ng 39t s electronegative so it pulls H s electrons away from H and to electrons Close to it Br a uuuuuu o Chemical Bonds between two or more atoms or molecules that are very close to each other due to induced dipole weakest interaction NOT a bond 2 T 39 Hydrogecn 9155M Hydrogen Bond R C 5 N R H 6 H I stronger than Van der Waals H O l lH O NOT a bond an interaction 0 a 5 between molecules with a partially positive 39339 0 0 Hydrogen atom bonded to a partially negative Rquot quot39R electronegative atom bond between oppositely charged ions cations and anions stronger than Hydrogen Bond NaCl a g i t A stronger than ionic sharing of electrons in outer level to fill outer shells of both atoms can be polar or non polar polarwater soluble NONpolar hydrophobicnot water soluble single double triple depending on atoms how many electrons needed for octet rule Single Double Triple bond bond bond H H OO N EN H H 636 Chemical Functional Groups Name Molecular Structure Molecular Structure Formula Formula Hydroxyl OH H II Amino NH2 I I I I H H II II II Methyl CH3 Carbonyl CO O T H Rc H C H CH3 H Carboxyl COOH u o Phosphate P04 391 I I 39 HCCOH 39 I t H II Ill Sulfydryl SH SH H30 H H 30f13 Macromolecules Large Biomolecules Carbohydrates Proteins Fats Lipids Nucleic Acids Polymers Repeated subunit many monomers come together to form a polymer Monomers subunit sugar monomer tor carbs amino acids monomer for proteins nucleotides monomer for nucleic acids lipids are NOT polymers so it doesn t have monomers MakingBreaking Down Polymers Dehydration reaction Makes polymers take out water and a covalent bond forms between monomers Hydrolysis Reaction Makes monomers water is added and the bond holding monomers together breaks Hp V HO Hoj 39 39 H Hf In H titerg l o rucrglquot x39 r 93 In C DH Hailr n c were on syruthesns Hydrolysm Energy made of sugars Polysaccharides Plant starch Animals glycogen Monosaccharide sugar 3carbon sugar Trioses 5carbon sugar Pentose 6carbon sugar Hexose Disaccharide glucosemonosaccharide fructose monosaccharide water gt sucrosedisaccharide bonded with glycosidic bonds Func ons most enzymes are made of protein drives metabolism 39 transport Polymer Polypeptides proteins can be made of many polypeptides Monomer Amino acid II II I I 39A lzm n39v39IJp Cl R L i 1 u Polypeptide chain protein dehydration reaction peptide bonds fold into 3D structure structure gives its function Primary Structure sequence of amino acids order in which amino acids are covalently linked Secondary Structure Hydrogen bond formation between atoms of backbone Betapleated sheet Alphahelix sheet Tertiary Structure depends on chemical bond between Rgroups mostly noncovalent Quaternary Structure 0 not all proteins have this only if there are more than one polypeptide chains Motif common element of secondary structure Domains functional units within a protein Folding and Denaturation chaperones proteins that help fold other proteins denature loses shape loses function heat denature acid denature Polymers DNA RNA Monomer nucleotides H H N H 039 I H 0 Pa CH Ao Nquqmous 39 o base quot quotl l 060mm Phowhnto H H O39WP 4of13 Extmph cl ammo sad when imam minivandon a vivaWM R a ca 0 NM 0 2 c W D O I C l Cu 0t Cu cu m C en but quotWM Tertiary Structure Bond in Nucleic Acids phosphodiester bonds 5 Carbon bonded to Phosphate group 3 Carbon bonded to top of phosphate group phosphate gt5 sugar 3 gtphosphate gt5 sugar DNA is always double stranded held together by Hbonds between base pairs C G A T antiparallel RNA is singlestranded U replaces T OH group replaces H on sugar hydrophobic energy storage Fats 50f13 not polymers but are made from smaller molecules bonded through dehydration reactions constructed of 2 smaller molecules glycerol and fatty acid glycerol 3Carbon alcohol with hydroxyl group attached to each carbon r H r H li C IE H OH OH OH fatty acid carboxyl group attached to long usually 1618 carbon skeleton acidic because of the carboxyl group Triglycerides 1 glycerol 3 fatty acids combine through dehydration the 3 fatty acids can be the same or different vary in the number of carbons and the presence of double bonds no carbon double bonds saturated these have ALL the hydrogens they could have they are saturated with hydrogens solid at room temp H fatty acid with one or more CC double bond unsaturated there could be more hydrogens if the double bonds weren t there cannot solidify oils are unsaturated H H C C l f l l n l II 3 II 3 l ZIT I D 1 1 D D l l p l r 1 ltr1 l I l D it I Unsaturated N l H H H H H H L I ll 0F r I l n 39 l I I I I H H H H H l A l l o Saturated Phospholipids two fatty acids one glycerol phosphate group at the end polar hydrophilic head nonpolar hydrophobic tail amphipathic molecule water liking part and water hating part phospholipids dropped in water form layer with fatty acid tails sticking up into the air phospholipids blended in water form a sphere where the surface is the head groups and tails are inside away from the water called a micelle another type of micelle vesicle phospholipid bilayer with heads facing the water and tails inside y 39 dwg J 4 g c yautt H II x x t J 52 I yyh vesicle c Mlcelle Other kinds of Lipids Terpenes found in biological pigments Steroids hormones 3h4 IIII Cell theory all living things are composed of cells life processes happen inside the cells metabolism heredity cells are compartments little bags of chemistry Prokaryotes karyote nucleus pro beforewithout prokaryotes are cells without a nucleus Eukaryotic Cells diverse developed internal membrane membranebound organelles Nucleus info center DNA codes for RNA gt RNA leaves the nucleus and then codes for protein in the cytoplasm RnftR Tv J iJL i 333 Q39 CMC aquot no u m l I N N N I H39 I 2 u I i I 2 I no r 39f 1r RNA moves out of nucleus through pores proteins are made in the cytoplasm but instructions are given in the nucleus proteins have signals signal sequence depends on the signal tags on the protein Ribosomes protein factories large subunit small subunit when protein leaves ER it is transported in vesicle and moves to golgi 2 Main Branches of Movement Ribosomes in Cytoplasm endoplasmic reticulum cytosol nucleus Compartments increase efficiency of reactions Aquaporin protein that allows H20 to pass through the membrane 1 300039 3925 000000 0000C 2 V JOOCCC Cytoskeleton networks of proteins and protein fibers that provide shapestructure of cells suppon mobility regulation 7of13 80f13 3 Main Types of Fibers microfilaments Actin protein subunit posneg ends microtubules tubulin dimers alpha and beta posneg ends intermediate filaments 50 different kinds nuclear lamina lines nuclear envelope Hydrophilic head fatty acid hydrophobic tail phospholipid bilayer proteins embedded hydrophobic sides hydrophilic inside and on top and bottom phospholipids can move lateral movement 10quot7 moves per second flipping happens once per MONTH this is because the hydrophilic heads would need to move through the hydrophobic tails to flip which would be very hard saturated fatty acid tails viscous hard to get through because there are no kinds and it is saturated with hydrogens unsaturated fatty tails fluid many kinks from the double bonds not too many hydrogens to get through Cholesterol based on its structure where would it be found if added to the phospholipid bilayer O H has a partial negative partial positive charge it is hydrophilic OH interacts with the hydrophilic heads Cholesterol while the rest made by cells interacts with modulates membrane fluidity hdeOPhObIC tallS Membrane Fluidity affected by many things 90f13 tails get more saturated with Hydrogen fluidity decreases 3 is gt E i a g temp increases E 0C9 fluidity increases g g D Q E E D E Temperature 3 5 as It gets colder fluidity g naturally decreases so the ac amount of cholesterol must g INCREASE to make the 39CE membrane more fluid D E amount of cholesterol at low temp Proteins in Membrane c Slmal tramducuon b Enzymatic activity atTransport What can get through membranes small non polar molecules some small polar molecules barely any large non polar molecules saturation of fatty acid d Collcoll rocognhlon foof13 NO ions or large charged polar molecules Membrane Transport 2 fundamental processes Passive Transport no energy needed diffusion Active Transport energy needed usually ATP Diffusion movement is always from high to low concentration DOWN a concentration gradient rate of diffusion depends on how big the molecules are increase size gt decrease rate temperature increase temp gt increase rate electrical charge like charges gt slow rate opposite charges gt fast rate concentration gradient the closer it gets to equilibrium the slower the rate gets Osmosis diffusion of water across a membrane based on solute concentration goes from low SOLUTE concentration to high SOLUTE concentration water moves toward the side with more solute particles tonicity ability of a solution to gainlose water isotonic solute concentration same on both sides hypertonic solute conc is higher outside the cell shriveled blood cell hypotonic solute conc is lower outside the cell big bursting blood cell Facilitated diffusion most things can t diffuse across a membrane these molecules are helped by channel or carrier proteins still moves from high to low concentration 0 0 0 o o 0 o 0 o 0 o o 0 0030mmquot quotgxxnxxxJc quot 39 l g 39 i 39 quot I s H y t 6 channel carrier moves molecules against concentration gradient requires energy primary active transport direct import of ATP secondary requires a gradient made by primary active transport fill uniport antiport Symport 11 of13 Primary Active Transport NaK Pump requires ATP to drive the pump carrier protein has a binding site that has a HIGH affinity for Na Na attaches to the binding site ATP then phosphorylates the carrier protein which changes the entire proteins structure the new structure faces the outside of the membrane and no longer has a high affinity for Na so the Na is released the new structure has a high affinity for K now so K attaches itself to the binding site the protein is then dephosphorylated and changes its structure again back to original structure opened to the inside of cell with high affinity for Na since it no longer has a high affinity for K the ions are released into the cell and Na bind pump leads to much higher Na outside and much higher K inside 3 Na ions out 2 K ions in Secondary Active Transport cotransport concentration gradient made by NaK pump allows glucose into the cell when Na goes in it takes glucose with it against its concentration gradient Endocytosis Phagocytosis Iqum I 17 Thu typos of mkxytous no annual all 39 eating Enuczuuun nun v o b 0 39 O O PinocytOSIs 0 0 0 o 0 O O Regelntlgrgnediated39 39 o O 39 39 p I V 39 receptor proteins Only accept 0 4 0 Y 1 target molecules 1 a pm 0 Yo on 0 M 0 poma a m 0 COM P Xxfo j 39 3 Como V O 4 x l mm 0 0 f0 1 ill moonwa lbl Momma lcl Rawmound mocytouc g VIC pJ Nr 39Mle c on N04 0 wH 0 0 Ch 6 Energy and Metabolism 2 Types of Energy Kinetic energy of motion Potential energy storedenergy of position Flow of energy thermodynamics track energy by using redox reactions transfer of electrons oxidation atom loses an e reduction atom gains an e Laws of Thermodynamics 1 energy cannot be created or destroyed can be changed 2 entropy is continuously increasing everything is getting more and more disordered G energy available to do work spontaneous reactions Delta G negative exergonic reaction energy is released reactions that require energy Delta G positive endergonic reaction energy is addedrequired Products teactantssubstrates gt endergonic reaction 12of13 ReWubstrates 0 Products gt exergonicspontaneous rxn To go from reactions to products the reaction has to get over the activation energy Ea E Reactanbsuljzates w Products AI Enzymes lower the need for activation energy uncatalyzed A Catalyze proteins that serve as biological catalysts enzymes bendstretch the bonds in the reactants so they break easier and become products faster reactantssubstrates bind to an enzymes active site like a lock and key and then the enzyme changes shape so that it fits even better 13 of13 after the substrate binds the products are released and the process starts over again with the same enzyme new substrate Factors that affect the rate at which the enzyme functions enzyme concentration substrate concentration if the amount of substrate increases the rate will increase until all of the enzymes are busy and going as fast as they can Then if the substrate concentration still increases the rate stays the same because they can t go any faster temperature enzymes have a certain temp that they function best at called optimum temp pH also have optimum pH regulatory molecules molecules that work with enzymes help the enzymes function V I 12 Vmax Km substrate concentration Km how quickly things get saturated affinity of enzyme for substrate competitive vs noncompetitive stop the enzyme from binding with substrate Companth inhib of untcr39cres WIquot active 5th of enzyme so wbtslrzuc r cartr ol bind sob g L g Enzyme Noncompetmve ml bulor changes shape of enzyme 80 It carnot and to Substrate a Compcumc nhzzxnon bl Noncompchtwc inhibition
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