Exam 1 BIO 1510 Study Guide
Exam 1 BIO 1510 Study Guide Bio 1510
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This 58 page Study Guide was uploaded by Nausheen Zaman on Thursday September 24, 2015. The Study Guide belongs to Bio 1510 at Wayne State University taught by Dr. Nataliya Turchyn in Summer 2015. Since its upload, it has received 415 views. For similar materials see (LS) Bas Life Mch in Biology at Wayne State University.
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Date Created: 09/24/15
BIO 1510 Study Guide for Exam 1 Chapters 25 Chapter 2 Main Points 0 Properties of Atoms 0 000000 Atomic Number Protons Neutrons Electrons Energy levels shells valence shellselectrons Isotopes Carbon 14 and Use Orbitals properties and how to calculate electrons in orbitals Ions Cations and anions OxidationReduction reactions Redox reactions Bonds and interactions 0 Properties of Water 0 pH Acids Bases and Buffers o Acidosis vs Alkalosis Atoms o Protons positive electrons negative neutrons neutral Atomic number of protons neutrons Atomic weight mass atomic number Atomic mass protons neutrons protons electrons neutrally charged particles only a Isotopes 0 atoms whose protons electrons but the neutrons are different 0 014 radioactive because more neutrons compared to protons in nucleus I C14 dating treating cancer and Alzheimer s Carbon Dating Level of C14 in an organism is compared to the level of C14 in the atmosphere All living plants and animals have a certain level of C14 in their bodies 0 C14 enters plants in the form of C02 0 Animals get C14 by eating plants 0 When an organism dies the C14 is the same is the C14 in the air stop taking in C14 0 Slowly decays to N14 0 Half life of C14 5730 yrs 0 Takes 5730 yrs for 50 of C14 to turn into N14 0 The longer the organism is dead the more N14 is present and less C14 is present 0 If a fossildead organism is more thanequal to 50000 yrs old another method should be used 0 Extended exposure can do severe damage to living organisms destroying our cells Energy Levels and Orbitals o Electrons have different energy levelsshells K L M N etc 0 Indicate the amount of energy the electron has 0 Farther from the nucleus more energy The of electron in the valence shell outermost shell of the atom determine chemical properties of an atom 0 Complete valence shell 8 e o If incomplete reacts with other atoms to complete shell o If complete chemically inertstable Electrons orbit around the nucleus in orbitals such as s p d f etc DO NOT CONFUSE WITH ENERGY LEVELS 0 areas around the nucleus where electrons are most likely to be found 0 Orbitals tells the physical location of electrons in an atom while the energy levels tell us how much energy an electron has 0 No orbital can contain more than 2 electrons 0 Formula gt 2nquot2 n of shells Atomic Ions Redox Reaction Electrons absorb light energy as they move to a higher level away from a nucleus Electrons release heatlight energy as they move to a lower level closer to the nucleus 0 The electron has to have more energy to keep the energy it had in the lower level every time it moves to a different level lons form when an atom losesgains electrons o Cations positively charged ions when electrons are lost of protons gt of electrons o Anions negatively charged ions when electrons are gained of protons lt of electrons OxidationReduction reactions 0 Oxidation loses e gains positive charge 0 Reduction gains e loses positive charge 0 Movements of electrons up and down energy levels is an oxidationreduction together ALWAYS redox reaction 0 OIL RIG Oxidation ls Loss Reduction ls Gain Chemical Bonds 0 Strongest to Weakest o Covalent gt Ionic gt Hydrogen gt Hydrophobic interaction gt van der Waals o Ionic Bonds 0 Form between two oppositely charged ions cations and anions 0 Le Table salt NaCl crystal 0 Na Sodium goes through oxidation while Cl chlorine goes through reduction I Na is a cation and Cl is an anion o Covalent Bonds 0 Two atoms that share one or more outer shell electrons o HH Single covalent bond WEAKEST o 00 Double covalent bond 0 NN Triple covalent bond STRONGEST I It takes more energy to break this kind of bond 0 Nonpolar equal sharing of valence electrons similar electronegativities I CH bond and CC bond are two examples of nonpolar covalent bonds 0 Polar nonequal sharing of valence electrons differing electronegativities I OH Bond an example of this Chemical Bonds Cont Chemical Reactions 0 Hydrogen bonds 0 H iS FON I H gt Hydrogen I F gt Flourine I O gt Oxygen I N gtgt Nitrogen 0 Form between hydrogen atom of one molecule and an electronegative atom O N or F of another molecule 0 Chemical Reaction 0 The formation and breaking of chemical bonds 0 The rate of chemical reactions depend on I Catalysts gt enzymes that speed upinitiate reactions I Temperature gt majority of chemical reactions occur higher temperatures I Concentrations of reaction vs products gt more reactants present quicker larger reactions Properties of Water Cohesive Adhesive High Specific Heat High Vaporization Frozen water less dense than liquid water Universal Solvent Organizes nonpolar molecules hydrophobic exclusion Forms ions 0 H20 gt OH anion H cation 0 AcidsAcidic solutions gt H gt OH ie lemon juicestomach acid 0 Neutral soultions gt H OH ie water 0 BasesBasic Solutions gt H lt OH ie bleachenzymes in small intestine Acids Bases Buffers pH logH lower pH lt7 gt higher H and lower OH stronger acid 7 gt pH gt 14 gt basic higher pH gt lower H and higher OH stronger base 0 Blood 74 pH weak base 0 Water 7 pH neutral 0 Buffers o Buffer a substance that minimizes changes in pH 0 Acts by donating H when the solution becomes too basic amp accepting H when it becomes too acidic o Carbonic acid works in blood bicarbonate buffer Acidosis vs Alkalosis o Acidosis o Occurs when blood becomes too acidic because of higher concentration of H 0 Blood pH falls below 735 0 Causes I Hypoventilation less breathing and exhalation I Pneumonia emphysema 0 higher 002 gt higher H2003 gt higher H o Decrease H in blood by adding bicarbonate ions decrease C02 concentration by inhaling more 0 Alkalosis o Occurs when blood becomes too basic because of higher concentration of OH 0 Blood pH raises about 745 0 Causes I Hyperventilation too much breathing exhaling more 002 than normal I Stress anxiety 0 lower 002 gt lower H2003 gt lower H Increase H in blood by adding carbonic acid 0 Increase COZ by placing paper bag over mouth and nose concentrates C02 inside paper bag 0 Chapter 3 Main Points Molecules MacroMicro 0 Types of MacroMicromolecules Functional Groups Monomers Polymers lsomers DNA Nitrogenous Bases Carbs o MonosaccharidesPolysaccharides Proteins 0 Polymers Special Amino Acids Lipids 0 Folding Steroids Fats MicroMacromolecules Molecules Micromolecules Macromolecules Carbohydrates Proteins Nucleic Acids Lipids Different Macromolecules o Carbs and Proteins o Carbs composed of simple sugars I Simple sugars building blocks for carbs ie glucose for energy I Starchglycogen store energy I Cellulosechitin structural support 0 Proteins are the most diverse of the macromolecules 0 Most proteins are enzymes help quicken chemical reactions 0 Amino Acids building blocks of proteins I 20 Amino Acids 0 Nucleic Acids and Lipids 0 DNA Deoxyribonucleic acid I Blueprint of life contains all info to construct an entire organism 0 RNA Ribonucleic acid I Used for gene expression 0 Nucleus contains the most DNA and RNA in our cells 0 Lipids Hydrophobic molecules nonpolar I Fats store energy I Phospholipids form cell membranes I Steroids include cholesterolsex hormones estrogen testosterone etc Functional Groups 0 What are Functional Groups 0 Certain groups of atoms in macromolecules that determine their characteristic functions Hydroxyl consists of an OH group OH Carbonyl Carbon double bonded to oxygen CO Carboxyl Combo of carbonyl and hydroxyl group acts as an acid by donating its H to a solution OCOH Amino Acts as a base by removing H from a solution HNH o H a proton because it has one proton and no electronsneutrons Sulfhydryl polar covalent bond with a sulfurhydrogen bond S H 0 Polar covalent because sulfur has higher electronegativity o Disulfide bridge covalent bond that forms between the sulfur atoms of two cysteines o Nonpolar because it forms between two sulfur atoms with similar electronegativities Phosphate group energy 0 Found in nucleic acids denoted as P Methyl group associated with proteins Carbon with three hydrogen atoms Carbs Proteins o Carbs 0 Starch polymers many monomers example of polysaccharide I Monomers building blocks of polymers I Monosaccharide simple sugar 0 Two monosaccharides disaccharide 0 Many monosaccharides polysaccharides I Animals cannot make starches but can digest them 0 Proteins 0 Two amino acids dipeptide 0 Many amino acids polypeptide chain I Peptide refers to a chain of amino acids held together with peptide bonds Polar covalent bonds link amino acids together Proteins usually made with twomore polypeptide chains I Myoglobin one polypeptide transportsstores oxygen in our muscles I Hemoglobin four polypeptide chains transports oxygen002 in our blood Proteins with one polypeptide Polypeptide 0 Proteins with twomore polypeptides NOT polypeptides Lipids Nucleic Acids Polymers 0 Nucleic Acid 0 Two nucleotides dinucleotide 0 Many nucleotides polynucleotides DNA and RNA 0 Lipids o Triglycerides fats I Not all lipids have fatty acids in their structures all have hydrocarbon chains I 0H and 00 are two nonpolar covalent bonds that are hydrophobic hydrocarbon chain I Carbonxyl group is acidic o Polymer made through dehydration synthesis water lost to make covalent bond broken through hydrolysis water molecule breaking up the covalent bond 0 Monomers 0 SC 5C 60 are all lsomers gt Same structure but arranged differently in space 0 Cs number clockwise from 1st 0 Disaccharides Polysaccharides o How are they Formed o Glycosidic Link unique to sugars covalent bond between monosaccharides o lmportantPolysaccharides 0 Starch Glycogen glucose molecules gt Store energy I Starch gt Plants I Glycogen gt Liver animals 0 Chitin Cellulose I Chitin gt Structure support animals I Cellulose gt Structure support for cell walls plants 0 Undigested fiber for humans DNA VS RNA DNA Type of Sugar Deoxyribose Double Stranded Double Helix Number of Strands Nifrogenous Bases Guanine G and Thymine T Bonds Phosphodiesfer and Hydrogen Bonds Adenine A Cy rosine C RNA Ribose Single Stranded Single Helix Adenine A Cy rosine C Guanine G and Uracil U Phosphodiesfer Bonds Purines and Pyrimidines Ribose vs Deoxyribose 0 Different Nitrogenous Bases o Adenine Guanine Purine I PURe As Gold gt PUR Purine A Adenine G Guanine I Purines Double ring structure 0 Cytosine Thymine Uracil Pyrimidine I CUTthe PIE gt C Cytosine U Uracil T Thymine PIE Pyrimidine I Pyrimidine Single ring structure 0 Adenine Guanine and Cytosine are in DNA and RNA 0 DNA has Thymine while RNA has Uracil o Deoxyribose vs Ribose o OH on 20 in RNA ribose o H on 20 in DNA deoxyribose 0 Remember deoxy gt without oxygen the deoxyribose on has a H attached to 2 C rather than OH group How to Recognize Nucleotide Groups 101 1Determine whether its a deoxyribonucleotideribonucleotide a REMEMBER Dexoribonucleotide gt deoxyribose gt H attached to 2 0 b REMEMBER Ribonucleotide gt ribose gt OH attached to 2 0 2 Determine whether nitrogenous base is purinepyrimidine c Purine gt double ringed include adenine guanine i Guanine carbonyl group ii Adenine no carbonyl group d Pyrimidine gt single ringed include cytosine thymine uracil i Cytosine one carbonyl group ii Thymine Uracil two carbonyl group iii Thymine has methyl group attached deoxyribose iv Uracil lacks methyl attached to ribose DNA Structure where a free is attached 0 O H rOXyl b0 nClS to the 539 C of one terminal g sugar also found in V39W c mm Wquot quotquotquotquotquot quotquot RNA Phosphate group o 5 and 3 ends are unique to nucleotides don t exist anywhere else Phosphodiester bonds covalent bond in which links two adjacent nucleotides extending from the 539 C of the sugar of one nucleotide to the 339 C of the sugar of the neighboring nucleotide o Nitrogenous bases don t form SugaPhosphm backbone consists covalent bonds they form H ofsugarsand phosphate groups bonds so they aren t involved in backbones of DNA and RNA 0 Phosphodiester bonds unique to nucleotides where a free OH is attached to the 339 C of another terminal sugar also found in RNA Another Important Nucleotide ATP ATP Adenosine TriPhosphate gt energy currency of the cell 0 AMP Adenosine MonoPhosphate gt used to make RNA very similar to ATP Has nitrogenous base adeninepurine Ribose OH group attached to 2 C ATP has three phosphate groups P group energy AMP has one phosphate group 0 ATP can donate two of their phosphate molecules to other molecules 0 Proteins 0 Proteins are the most structurally diverse of all macromolecules 0 Function as enzymes defense systems transport support motion function regulators and storage 0 What are Protein made of 0 Made of one or more polypeptide chain gt made of amino acids H2N gt amino groupN terminus COOH gt carboxyl groupC terminus All attached to central carbon R group differs between amino acids 20 different R groups 20 different amino acids I R group determine chemical properties of amino acids 0 Peptide bonds linked through dehydration synthesis Special Amino Acids o Proline gt causes polypeptide chain to bend o Methionine gt first amino acid to make proteins 0 Cysteine gt Contains sulfide group to participate in formation of disulfide bridge OOOO Classes of Amino Acids o Nonpolar Amino Acids o Nonpolar R groups contain H and C atoms gt nonpolar bond 0 R group nonpolar gt entire amino acid nonpolar I Methonine is nonpolar gt 80 bond nonpolar o Aromatic acids benzine rings contains six Cs 0 Polar Amino Acids 0 Polar R groups gt O is present in structure I OH C N and 8H bonds polar o Hydrophilic like water 0 Tyrosine only aromatic amino acid in this group contains benzine ring o Chargedlonizable Amino Acids 0 Charged R groups I Charge of R group charge of amino acid I charge amino acid basic I charge amino acid acidic I ALL CHARGED AMINO ACIDS ARE POLAR 0 none are aromatic Polypeptide BondsStructures 0 Folding of Polypeptides 0 Primary structure nonfunctional I Can become a beta pleated sheetalpha helix sheet secondary structure 0 HBonds formed in secondary structure I Secondary structure nonfunctional I HBonds form between amino acids in polypeptide chain between 0 of one amino acid and H in another amino acid 0 Difference between secondaryprimary bond I Secondary gt contains HBonds Primary gt NO HBonds I Both structures have covalent bonds 0 The Final Stages of Folding o Tertiary structure overall 3D shape of polypeptide 0 Forms from interactions between R groups of various amino acids I Polypeptide chain assumes a 3D shape I May form additional bonds van der Waals HBond Disulfide bridge etc I Because of additional bonds polypeptide folds o Quaternary structure arrangement of two or more polypeptide chains subunits in space I Can be held by ionic bonds disulfide bridges etc I Folded proteins functional I Unfolded proteins nonfuctional Polypeptide BondsStructures Con Chaperons Denaturation vs Dissociation o Bonds that Make Polypeptides Fold 0 Fold because of additional bonds within Amino acid I van der Waals gt attraction between atoms within a short distance because of fluctuating electrical charges I Hydrophobic exclusion gt hydrophobic R groups of amino acids stay together excluding themselves from water 0 Disulfide bridge is strongest polar covalent bond of all bonds 0 Disulfide bridge gt Ionic gt Hydrogen gt Hydrophobic exclusion gt van der Waals o Chaperons HSP high shock proteins that assist with folding protein correctly 0 Denaturation vs Dissociation o Denaturation protein unfolds denatures because of exposure to heatchemicals I Protein has twomore polypeptides gt loses quaternary tertiary secondary structure I Protein has one polypeptide gt loses tertiary secondary structure 0 In some cases denaturation can be reversed upon removal of denaturing agent renaturation Lipids Fats Triglycerides Phospholipids Steroids Choles rerol Estrogen V Testosfer39one Fats o Fats Triglycerides o Consist of 3 fatty acids linked to one glycerol BC polyalcohol 0 Each fatty acid has hydrocarbon chain acidic carboxyl group 0 Two type of fatty acids I Saturated fatty acid no double bonds between C atoms I Unsaturated fatty acid 1 or more double bonds 0 Monounsaturated 1 double bond between C atoms 0 Polyunsaturated 2more double bonds between carbond 0 Why do unsaturated fats take up more room than saturated fats unsaturated fats have hydrocarbon chains that have double bonds Double bonds cause the hydrocarbon chains to bend o Cis Fats vs Trans Fats o Unsaturated fats can be cistrans fats o Cis fats have hydrogen atoms present on one side of the double bond I both hydrogens can face up or down on double bonded carbons 0 Trans fats have hydrogen atoms on opposite sides of the double bond bad for us I H bonds in fats increase cholesterol levels in our blood Fats store energy glycogen also stores energy in liver amp muscle cells Saturated fats solid room temp hydroC bonds don t bend allowing them to stay straight and close together I Butter 0 Unsaturated fats liquids room temp hydroC bonds bend preventing them to pack close together I Olive oil Steroids Steroids Cholesterol 0 0 Found in animal cell membranes Makes cell membrane less permeable to water soluble molecules wo it membranes will be more fluid and molecules will pass through cells easier No fatty acids in structure 4 hydroC rings HydroC chain hydrophilic functional group hydroxyl HDL highdensity lipoprotein has more proteins in structure good cholesterol LDL lowdensity lipoprotein has more cholesterol in structure bad cholesterol LDL sticks to veins and arteries blocking them gt arterosclerosis hardeningnarrowing of arteries leads to heart attackstroke I Heart attack when heart muscle is destroyeddead Steroids o Steroids Sex Hormones o Testosterone male sex hormones I promotes development of male sex characteristics growth of body hair increased bonemuscle mass 0 No fatty acids 4 HydroC rings hydroxyl amp carbonyl group I Produced by testes o Estrogen female sex hormone I promotes development of female sex characteristics breast growth ovary development I Has two hydroxyl groups instead of one hydrophilic PhospholipidsBilayers o Phospholipids 0 Form all biological membranes plasmainternal membranes I Plasma surrounds cells I lnternal surrounds organelles Head hydrophilic Tails hydrophobic Amphipathic lipids phospholipids steroids Fats entirely hydrophobic Head hydrophilic bc of phosphate and other groups 00000 c Micelles and Lipid Bilayers o Micelles monolayered structures that form by adding detergents lipid like molecules to water I Detergents have only one hydrophobic tail phospholipids have two 0 Phospholipid bilayer more complicated structure where 2 layers form I Hydrophobic heads facing outward I Hydrophobic tails facing inward Chapter 4 Main Points 0 Prokaryotic o Unicellular organisms without nucleus 0 Eukaryotic 0 contains nucleus 0 Animal vs Plant cell I Organelles of plant and animal cell 0 Functions of organelles o Endosymbiotic theory 0 Junctions between cells Cells 0 Prokaryotic before nucleus 0 Lack nucleus 0 Unicellular o Eukaryotic have nucleus 0 Unicellular eukaryotes some protists yeast unicellular fungD o Multicellular animals plants all fungi gt 2 cells Prokaryotic Bacteria Archaeans Eukaryotic Protists w Plants Bacterial Cell 0 Bacteria o Separated into gram positivenegative I Gram positive purple stain 0 Include streptococcus 0 Cell wall contains thick peptidoglycan layer polysaccharide pep des I Gram negative no stainlight pink stain 0 Include E Coil 0 Cell walls contain lipopolysaccharides polysaccharides with lipids other materials covering thin peptidoglycan layer 0 Peptidoglycan targeted by penicillin disrupts cross linking between peptides that normally reinforce bacterial cell wall 0 Archaeans have no peptidoglycan in cell walls allow bate ium to attach to different surfaces Pill Cytoplasm semifluid matrix that contains macromolecules and ribosomes Ribosomes non membranebound organelles that are involved in protein synthesis Nucleoid Iquot region where bacterial DNA is located 7 39 s V Plasma membrane I encloses the cytoplasm o 39 Capsule provides an extr layer of tion I l Flagellum helps bacterium mo 39 around Cell wall protects the cell maintains its shape and prevents excessive uptake or loss of water Animal Cell 0 Animal Cell O 0000 Eukaryotic Nucleus surrounded by nuclear envelope ER has hollow interior gt lumen Inside ER gt worm like proteins Every animal cell has two centrioles I One centrosome microtubule organizing center gt a place where microtubules seperate chromosomes during cell division grow from H202 gt hydrogen peroxide All organelles are surrounded by internal membranes except for ribosomes Have no cell wall surrounds nucleus Nuclear envelope Nucleus membranebound organelle Rough endoplasmic where majority of DNA and reticulum REP RNA are found membranebound organelle 39 Smooth endoplasmic wnth ribosomes attached re mum SER Ribosomes membranebound non membmnebound I organelle wrthout organelles involved in quot 39 protein synthesis cytophsm Centrioles V made of microtubules Golgi apparatus Lysosome membranebound organelle consistin of stacks of membranebound vesicle atter sacs 22ml fOOd and Old Plasma membrane Peroxisome 7 membranebound organelle Mmehondmm which contains enzymes that membranebound organelle where produce H202 and split it into quotWWW 0 ATP is Pr OdUCBd H20 and 0 Plant Cell Nucleus 39 4 Nuclear envelope Rough endoplasmic Smooth endoplasmic reticulum RER reticulum SER Central vacuole I membranebound vesicle that stores H20 and waste products Peroxisome Chloroplast membranebound organelle where sugars are made Cell wall made of ceuulose Adjacent cell wall Plasma membrane Plant Cells 0 Eukaryotic 0 Have animal cell organelles in addition to I Cell wall made of cellulose polysaccharide Chloroplast Central vacuole plant cell can survive in dry conditions Have no centrosome with centriole not all have lysosomes Fungi cell walls made of chitin Some protists have cell walls made of cellulose Nucleus Ribosomes o Nucleus O 0 Nuclear envelope double lipid bilayer Nuclear pore allows molecules to go through nucleus Chromatin makes up chromosome Nucleolus ribosomal RNA combine with proteins to form small and large ribosomal subunits o Ribosomes O O Cell s protein synthesis machinery Each ribosomal subunit is composed of rRNAs and proteins Translation when ribosomes work together with messenger RNA 0 Nuclear pores Cytoplasmic filaments Nuclear pm CopyrightgTheMchwHillCompmieancquot 39 39 1 39 quot displuy Copyright 9 The MoGraw Hill Companies Inc Permission required for reproduction or display Large subunit Ribosome Small subunit Rough ERSmooth ER RERSER Copyright 9 The McGrowHill Companies Inc Permission required for reproduction or display 0 Rough Endoplasmic Reticulum ER 0 0 Synthesis and modification of proteins Glycoproteins proteins with short sugar chain produced in lumen of Rough ER White blood cells have high concentration of rough ER cells I Used for antibody production proteins 0 Smooth ER Smooth endoplasmic reticulum O O O 0 Synthesis of lipids Storage of Ca2 in muscle cells Detoxification of drugspoisons in liver cells No ribosomes gt can t make proteins gt makes lipids ie fats phospholipids and steroids Cells in ovariestestes abundant in smooth ER Rough endoplasmic reticulum RED Ribosomes Smooth endoplasmic reticulum SEQ Golgi Apparatus Copyright 9 The McGrawHill Companies Inc Permission required for reproduction or display 0 Transport vesicle amp o O Fusing i vesicle o Secretory vesicle o o Golgi Apparatus Functions in packaging distribution and additional processing of molecules Cis face removes proteinslipids from ER proteins from rough ER lipids from smooth ER Glycolipids lipids with short sugar chains Lumen in Golgi transformsmodifies proteins inside GA tubes Secret Pathway 0 Secret Pathway 0 To move proteins RER and lipids SER from ER gt transport vesicle Golgi gt secretory vesicle plasma membrane gt outside of cells 0 Transport vesicle is NOT an organelle membrane bound pocket derived from internal membrane V 39 o Secretory vesicle derived from Golgi 31 2u 1 3 39 membrane diffuasfhrwgh m whoHmquot 0 Process of releasing proteins andor lipids from cell secretion Exocytosis to exit cell Secretory proteinslipids released from cell the cis face of the Golgi Ms l l l 2 v Exfmcdluia39 fluid LysosomeCentral Vacuole o Lysosomes o Membrane bound digestive vesicle I enzymes of lysosomes proteins from rough ER modified in Golgi I work best in acidic pH higher H o Lysosome can digest damaged mitochondriaany other damaged organelle 0 Central Vacuole Plant Cells 0 Membrane bound vesicle in plant cells 0 Stores water in plants plants can survive longer in drier conditions I Gains water expands I Loses water shrinks Tonoplast membrane enclosing central vacuole Protists have contractile vacuoles regulate H20 balance 0 Food vacuoles digest food MitochondriaChloroplasts o Mitochondria 0 Missing in some protists 0 Makes ATP 0 Semifluid matrix 0 Cristae surface area of inner membrane 0 Chloroplasts o Algae have chloroplasts o Mitchondria chloroplasts found in plants only mitochondria found in animals 0 Makes sugars using solar energy aka photosynthesis Semifluid stroma Thylakoidthylakoid disks Thylakoid membrane covers thylakoids contains chlorophyll I Chlorophyll needed to cause photosynthesis o Stromathylakoid membrane are 2 places where photosynthesis occurs 0 Granum stack of thylakoid that increases surface area 9 39 Ribsomes Thylakoid membrane Inner membrane Outer membrane Outer membrane Intermembrane Inner membrane RIbOSOmes DNA CK VY39ll C luv Ik m re va umrx Tn t nuxuxu 39wpnul M nzn I 1x Chloroplast Eukaryotic cell with chloroplast and mitochondrion Endosymbiosis Eukaryotic cell with mitochondrion Aerobic bacterium EndosymbiosIs Internal membrane system Ancestral eukaryotic cell Endosymbiotic TheoryProof Endosymbiosis living together in close association Mitochondria derived from aerobic bacteria oxygen using gt engulfed by larger cell gt became a part of cell overtime Chloroplast derived from cyanobacteria gt engulfed by prokaryotic cell gt eventually became chloroplast Proof 1 Both mitochondria and chloroplasts surrounded by two membranes 0 Outer membrane gt derived from inner membrane of bacteria 0 Inner membrane gt outer membrane of cell 2 DNA inside mitochondria and chloroplasts bacterial DNA in size and shape 3 Ribosomes inside mitochondria and chloroplasts bacterial ribosomes 4 Replicate by binary fission not mitosis o Binary fission division in half from asexual reproduction found in bacteria Cytoplasm 0 Network of protein fibers found in all eukaryotic cells 0 supports the shape of the cell 0 keeps organelles in fixed locations Microtubule 0 involved in cell movement and movement of materials and organelles within cells o Cyto cell 0 Skeleton supporting structure o Smallest gt largest Intermediate filament Actin filament microfilament Cequot mettlbm e o Actin filaments gt intermediate filaments gt microtubule Filaments o Actin Filaments o Maintains cell s shape Assists in cell movement like crawling and contraction Each sphere represents a globular protein actin In our muscles actin myosin reaction allows muscles to move White blood cells fight pathogens use actin filaments to move by crawling out and into blood vessels 0 Amoebas use active filaments to crawl o Microtubules o Supportshape cell 0 Involved in movements of vesicles and organelles in cell 0 Guide movements of chromosomes during cell division 0 Microtubules hollow tubes composed of globular proteins tubulins alphabeta Both dynamic structures Reassembledisassemble easily Intermediate Filaments 0 Made of fibrous proteins don t break down easily 0 Maintains cell shape 0 Supports nuclear envelope OOOO Motor Proteins Vesicle o Microtubule highway motor proteins trucks 0 Two types of motor proteins 0 Dynein o Kinesin 0 Use ATP to move cargo vesicle organelle m Dynac n an 39 complex V Dynein 0 t C Microtubule Flagellum and Cilia Outer microtubule pair x A V V 0 IV V r V r J f r39 K a f gt 4 r V J f r V t n J h V A VJ J 39 39 Radial spoke 0 92 arrangement of microtubules o Centriolebasal body have 90 arrangement of microtubules o Cilia numerous short hairlike structures that allow some protists ciliates to move around Flagellum o In our respiratory tract ciliated epithelial membrane Ot m cells move mucus containing trapped 1 Cam 8wquot b d7 microtubule pair dust particles dead cells toward the throat to be swallowed eliminated from the body 0 Flagella long taillike structures that allow cells to move ie sperm cells some protists a 017m Microtubule triplet Outside AnimalPlants Cells Coagen Elastin 2 F ibronec n 39 Actin filam Cytoplasm Primary wall Plasmodesmofa secondary WCquot Plan cell Plasma membrane Animal cells 0 Extracellular matrix Organizes cells in tissues supports plasma membrane communicates with cytoskeleton Composed of o Fibrous proteins collagen elastin Glycoproteins Fibronectin o Proteoglycans proteins with onemore polysaccharide chains attached Plant Cells 0 O Primarysecondary cell wall made of cellulose Primary cell wall stretches secondary walls don t 2nCI wall has cellulose and lignin organic polymer that provides strength All plants have primary wall but not all plants have secondary wall Middle lamella hold plant cells together rich in carbs Cell Junctions o Tightjunction o connects plasma membranes of adjacent cells in a sheet to prevent materials from moving between them 0 Formed in epithelial cells in digestive tract preventing material from leaking into surrounding tissues 0 Anchoring junction 0 Cytoskeletons of two cells connected together with help of proteins 0 Proteins adherins I Connected to intermediate filaments of both cells with help of adherins 0 Found in tissues that stretch often muscles skin 0 Gap junction 0 Formation of gap between plasma membranes of two different cells I Gap made of proteins called connexions o Allows movements of ions small sugars and amino acids from one cell to another 0 Found in many different tissues heart muscle cells Plasmodesmata Primary Middle lamella Plasma cell wall membrane 0 Cytoplasmic connections between two neighboring plant cells 0 Similar to gap junctions in animal cells 0 Allows ions sugars and amino acids to be shared between cells 0 Different from gap junctions because they are line with plasma membrane and don t use connexions Chapter 5 Main Points 0 Membrane Structure 0 Membrane Proteins o How they associate with lipid bilayer 0 alpha helices and beta barrels 0 Passive and Active Transport between membrane 0 Osmosis Membrane Structure 0 1 39N McCrame Ccn Per to townie 0 reproducicr or G scaly amp Extracellular fluid k W Collagen ECM N J UV Glycolipid VJ l I g g M 4 a J 39 7 A J I I fz Glycoprofeins 4 3 3939 39 q quot o 1 I quot Integral g 39 quot transmembrane proteins 3 quotN fi men roskele ron 0 I quot1quot39 wm v a 39 o if Cytoplasm Actin filaments Peripheral proteins cytoskelefon Transmembrane proteins extend completely through lipid bilayer 0 Made of nonpolarpolar amino acids Peripheral proteins found on the extraintracellular sides of the membrane Animal cell membrane contain cholesterol ampiphacic Sugar groups on glycoproteinsglycolipids are found exclusively on the extracellular side of membrane involved in cell identity Membrane Proteins Transporter transports molecles and ions Enzyme catalyzes chemical reaction by alternating reactant Receptor something that recieves a signal 0 Signal ligand triggers a series of responses within the cell itself ie insulin I Only insulin receptors in certain cells like liver skeletal muscle and fat cells respond to insulin Substrate molecule by which enzyme acts Product may eve become a substrate in another part of the cell Cell surface identity marker uses glycoproteins Celltocell adhesion uses coadherins Attachment to cytoskeleton uses integrin ECM Association with lipid bilayer in two ways 0 Phospholipidanchored proteins attached to either side of membrane to onemore lipid molecules 0 Peripheral proteins interactions with membrane through noncovalent bonding to nhor nrnl39oinc Alpha Helices and Beta Barrels Transmembrane proteins extend across the bilayer as single a helix multiple a helices or bbarrel rolledup beta sheets 0 Majority of membrane proteins are in this category Alpha helices 0 Alpha helix passes lipid bilayer only once 0 Form because of hydrogen bonds 0 Amino acid side chain R group I Acts as a receptor 0 Extracellular part binds signal while intracellular parts signals to cell interior Beta barrels 0 Secondary structures of Alpha helices Multiple alpha helices and beta barrels form hydrophilic pores o Hydrophilic pores channels that allow H20 soluble molecules to move across lipid bilayer o Hydrophilic R group faces inside alpha helices Passive Transport 0 Movement of molecules down their concentration gradients no energy needed 0 Three types of transport 0 Simple diffusion I Allows molecules to cross membrane without membrane proteins no energy needed I Molecules move to lower concentration side of membrane I Equilibrium reached when equal number of molecules on each side 0 Facilitated diffusion I Cross with help of membrane proteins channelscarriers 0 Channels integral proteins that create a specific hydrophilic pore for specific ions 0 Carriers integral proteins that change shape to allow passing polar molecules through the membrane sugars amino acids some ions used to go through lipid bilayer I ie sodium ion channel 0 Osmosis I Diffusion of water down cncentration gradient I Aquaporins accelerates water movemtn across bilayer I Water always moves from the regions where its concentration is high and concentration of solutes is low to the region where its concentration is low and concentration of solutes is high I Water is solvent likes to dissolve solutes Solutions of Osmosis and Plant Cell Osmosis o Isotonic same concentration of solutes has same solutes as cell 0 Cell volume doesn t change 0 Hypotonic below concentration of solutes has much lower solutes than cell 0 Cell has more solutes than surrounding solute cell swells and it can burstlyse 0 Le distilledpure water 0 Hypertonic above concentration for solutes 0 Cell has less solutes than solution looses water and constricts 0 Le salt water 0 ln Plant cells 0 Hypertonic plant cell loses water plasma membrane shrinks away from the cell wall shriveled o Hypotonic H20 rushes in normal plant cell is usually swollen with water Turgid I Plant cell does not burst in Hypotonic solution because of cell walls 0 Isotonic solution in plant cell flaccid Active Transport OMquot 0171 W93 gtI CI YW ht Pun5w WIN t1 quotwtMm 0 Im 0 Movement of molecules up their concentration gradients with help of energy 0 Concentration gradient molecules V Iquot O Intracellular move from regions of lower J rammmmvmm 6 Dephosphorylation of protein triggers macaw mum concentration to regions of hIger maggmgegrmmm 2 39 39quot the celt and the cyde repeats concentration a Carriers used in active transport 0 Example Sodiumpotassium pump 0 ATP hydrolysis to move 3 Na ions out the cell and 2 K ions into cell against 3 Phosphorytation causes 5 Binding 039 poms oontormationitl chagoin pm 39 39 39 39 m quot593 reduci 39 a ini or 39a39 39a CO ncentratl on gra d le nt Mmspmwtamn 039 protein I I v then 33501th 4 This contormatlon has higher af nity o o tor K Extracellular potassium binds 0 More Na Ions outSIde rather than made the quotquot quot s cell o Less K outside than inside the cell
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