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Cell Biology, Exam 1 Study Guide

by: Pratiti Ghosh-Dastidar

Cell Biology, Exam 1 Study Guide BIO203

Marketplace > Miami University > Biology > BIO203 > Cell Biology Exam 1 Study Guide
Pratiti Ghosh-Dastidar

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Covers: Cell Theory Diversity of Cells Unity of Cells Prokaryotic v. Eukaryotic Cells Important Organelles in Eurkayotic Cells Characteristics of plant cells Types of Bonds Water and ...
Cell Biology
Dr. James
Study Guide
cellular biology, Cell, study, guide, exam, 1
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This 17 page Study Guide was uploaded by Pratiti Ghosh-Dastidar on Monday September 19, 2016. The Study Guide belongs to BIO203 at Miami University taught by Dr. James in Fall 2016. Since its upload, it has received 116 views. For similar materials see Cell Biology in Biology at Miami University.


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Date Created: 09/19/16
Pg -1 Cell Theory  Every living is composed of one or more cells  Whatever cell can do, gives a multitude of cells (tissue) a particular function  creating organ  organ system  Fundamental unit of life  Cells arise from pre-existing cells. Cells are Diverse  Allows for different functions  How ? o Size range < 1µM -- >200µM o Shapes  Nerve cell which has long cellular extension  Paramecium which is covered in cilia  Chlamydomonas : photosynthesis  Helicobacter pylori: Use flagella o Presence of a nucleus  prokaryotic v eukaryotic. o Presence of cell wall  For plants: cell wall gives plant shape and rigidity o Independent Vs. member of community  Humans (~ 37.2 trillion cells)  work together in a community  Yeast (cells survive independently) o Motility  ecoli uses flagellum to move around o Chemical requirements  Some require complicated mix of organic inorganic compounds to survive. o Function (e.g. humans)  Muscles  Digestive  Nerves  Renal  Estimated > 200 cell types in 4 tissue types humans Cell Unity  Different but the same o Cells store generic info as DNA (which is made of 4 types of nucleotides A-T/C-G)  sequence provides the info.  Replicate DNA by template polymerization o We know a pairs W/T(and C W/G) o Creates a tplate to allow to create different sequence  Transcribe genetic info – RNA o Dif cells (e.g. cardiac vs renal) will translate dif RNA sequences to create amino acid sequence (dif proteins which allow for dif functions).  Use protein catalysis o Speeds up chem. Rxns by lowering activation energy w/o prematurely modifying the protein (or enzyme) o Used to regulate genes  Synthesize biological macromolecules from subunits o Which are monomers (monosacrides, lipids, amino acids etc.)  Are enclosed in a plasma membrane  Require free energy  Regulate genes Prokaryotic cells Eukaryotic  Before nucleus  True nucleus  Photosynthetic, non-photosynthetic  Plants, animals, fungi archea  Characteristics  Usually larger than prokaryotic  Some live independently  Have membrane bound nucleolus  Variety of other organelles  3 divisions of this cell:  Plasma membrane  Nucleus  Vp  There is no nuclear bond nucleus Prokaryotic cells characteristics  Small (few microns)  Reproduce quickly (in optimum condtions)  Shape o Spherical o Rod shaped  Unicellular, but can grow in clusters (or chains)  Tough cell wall  No internal membranes  DNA is nucleoid – not membrane bound  Limited cytoskeleton Nucleus  Double membrane with double bilayer phospo-lipid  Contains most of DNA in cell  in the form of chromosomes  As cell moves through cell cycle  DNA becomes more and more condensed Mitochondria  Enclosed in 2 membranes  inner membrane folds into interior  Produces majority of ATP  contains its own DNA  Reproduce by division  Thought to have developed form bacteria Endoplasmic reticulum  Complex membrane bound compartments  Synthesizes most cell membrane components and materials for export  Part of the endomembrane system  connection flow of material from nucleolus all the way to plasma membrane  Rough synthesizes ribozomes Golgi apparatus  Stacks of membrane bound disks  Receives materials from ER  Modifies materials made in ER  Package materials for export from cell and transport to other cell compartments. Additional Organelles  Lysosome intracellular o Small, irregular shape o Membrane bound o Intracellular digestions  Transport Vesicles o Small membrane bound o Move materials between membrane bound compartments  Peroxisomes o Small membrane bound o Contains H O (hydrogen peroxide) which is used to inactive toxic 2 2 molecules.  Endocytosis material imported to cell o Membrane pinches and forms vesicles, endosomes take to lysosome.  Exocytosis transport vesicle buds off with plasma membrane Cytosol  Inside plasma membrane but outside organelles: gel-like  Aqueous solution/suspension of organic and inorganic molecules Cytoplasm  System of proteins filaments in cytosol  Controls cell shape, provides strength to cell, drives movement of cell and components Actin filaments (thinnest)  Abundant  Movement of cells and contraction Microtubules  Thickest hollow tube  Guide movement of intracellular components.  Form network for chromosomes segregation during cell division Plant Cell Plastids  Double membrane bound  Site of storage of important compounds Chloroplasts  Large green organelle  Surrounded by 2 membranes  Internal stacks of membranes  contains chlorophyll  Photosynthesis (use energy of sunlight to produce sugar)  Evolutionarily came into cell and via phagocytes Plant Cell  Vacuoles o Fluid filled o Storage provides turgor pressure (allows plant to be rigid)  Cell wall o Support structure Chemical components of cells (ch 2/4)  An atom simples unit of an element o Composed of subatomic particles  Protons and neutrons  Electrons  Atomic#; weight  An element chemical reactivity depends on ..? o Depends on whther the outer electron shell is full or not  HCON(elements) make up of the majority of life  Chemical RXNs form compounds of molecules (w/dif. Element) Bonds  Ionic bond transfer e -  - Covalent bond share e Electronegativity – measure of the tendency of an atom to attract a bonding pair of electrons  The higher the number, the grater the tendency Covalent bonds  Non-polar: when both atoms have similar electronegativity  Polar: unequal electronegativity. E.g. Oxygen has higher electronegativity than hydrozen  Hydrogen bonds very weak however macro molecular retail shape and structure because of Hydrogen bonds. Water o Noncovalent o H is covalently boded to electro negative O or N; interacting with electronegative O or N. o H 2 molecules can bind w/ up to 4 other H O 2olecules (or other polar molecules) via H-bonds.  Atoms within one large molecules o H bond stabilizes secondary structure of acids (maintains 3-D shape)  Atoms in 2 different large molecules o Binds dif. Bases of DNA (dif strands of DNA) o Hormone and receptor o Multimeric protein subunits  Life arose in H O 2  70-90% of live tissue in H2O  Biological systems – aqueous systems  Polar molecule o Forms H-bonds  Hydrophobic o Minimizes # of interaction and disruptive effect with H2O molecules. o Creates “a shell” around the hydrophilic molecule w/ h2) molecules  minimizing interactions. o Note: no repulsive force  H2O drives molecules to interact with other hydrophobic molecules Carbon 4 valence electrons  Uses those electrons to dictate how many and the types of interactions it can have with other atoms o Share 4 electron pairs o Form 4 bonds  4 single bonds  Or 2 single bonds 1 double bond  Thus allowing the formation of large, complex molecules o Can form chains, branched trees and rings  Chains: theoretically no limit to size of chans.  Often all these conformations can be formed together to make large variety of complex structure. Hydrocarbon: molecules composed of only hydrogens and carbons Organic: Carbon based structure which interacts w/o the carbons, hydrogens and oxygens  Hydrogen typically hydrophobic  Functional groups: a particular type of atoms which give a particular chemical characteristic. Hydrophillic  Amines - base group  Sulfhydryl  can form sulfide bonds  Phosphate: o Inorganic phosphate o Organic phosphate  Proteins are modified via phosphylation II The four biological macromolecules 1. Polysaccharides 2. Fats and membrane lipids 3. Proteins 4. Nucleic acids  Made of subunits (monomers) to make these macromolecules Monomers  Polymers Of 30% chemicals in bacteria Sugars (simple)  polysaccharides 2% Fatty acids  Fats/Membrane lipids 2% Amino acids  Proteins 15% Nucleorides  Nuclic acids 7% Hydrolysis (Splits apart)  H2O is split to split macromolecule  Carbohydrates = monosaccharide + polysaccharides o Important for energy storage & structural purposes  Subunit monosaccharide  short term energy storage  Polysaccharides long term energy storage – used also structural purposes Monosaccharide Disaccharides (forms glycosidic bonds)  Many sugars are isomers of each other o Have same chemical formula but different spatial arrangements o Relative to plane of ring structure, OH group can switch (important in starches)  Sugar derivatives o Can add different functional groups (like amines, acetate etc.)  Disaccharides: 2 covalently linked monosaccharide via condensation rxn (forms glycosidic bond) o Αlpha-glucose + β- fructose  sucrose o Sucrose (glucose + fructose) o Lactose (glucose + galactose) o Maltose (2 glucose molecules)  Polysaccharides – biological macromolecule  many monosaccharides linked via condensation reaction in either straight or branched chains. o Long term energy storage o Complex carbs (structures)  Ex. Cellulose (not digestible),  glycogen,starch  digestible Pg – 12  Starch (all glucose in Alpha config) making 1- 4 linkage of Alpha glucose  Cellulose (all glucose β – config) making 1-4 linkage of β – glucose Oligosaccharides  Highly branched  Found: o Extracellular face of cell membrane o Extracellular cell matrix o Glyco proteins and glyco lipids Peptiglycans (ex of polysaccharides)  Found around bacteria o Gram positive  Serves as protective role and preserves shape of bacteria Lipopolysaccharides  Gram neg bacteria  Contains a lipid portion w/ 2 curb layers. Chitin  Found in arthropods and fungi  Glucosamine bonded via glycosidic bonds Glycoproteins & glycolipids  Found in cell membranes  Some partially, some fully embedded in membrane o Help cell recognize what molecules approaching, extracellular matrix and signal communication. Lipids  Macromolecules but not polymers  Hydrophobic o Insoluble in water  Types o Fats o Waxes o Sterols o Oils o Phospholipids  Found in membrane hormones and vitamins o Used as very long term energy storage o Insulation  Classes o Lipids w/ fatty acids o Lipids without fatty acids Composition: hydrophilic carboxylic acid head + hydrophobic hydrocarbon tail  Hydrocarbon tail o Usually 16-18 carbons in length o Saturation  Unsaturated molecules: have double bond(s) which create a link in the hydrocarbon chain  Saturated molecules: all bonds are single. Eg. Oleic acid has one double bond, steric acid has only single bonds Lipid with fatty Acid: Triacylglycerol  Fats and oils o Long energy storage o Insulation  Phospholipids o Found in membranes Triacylglycerols  to link: dehydration reaction  to make : glycerol + 3 fatty acids  triacylglycerols  overall hydrophobic o in H2O hydrophobic interactions causes it to separate  higher entropy of b/c of lower surface area of molecule, allow more H2O molecules to move around and less surrounding the molecule in orderly structure.  not carbohydrate b/c not right structural formula  efficient energy storage (9300 cal/g)  fats v. oil o fats have saturated fatty acids  solid at room temp b/c chains can pack together tighter more interactions b/w molecule adjacent molecules  animal some plants o oils have unsaturated  double bonds causes links  less interactions, less tightly packed  liquid at room temperature  mainly plants and fish Phospholipids  glycerol + 2 fatty acids + polar group phosphate  similar composure/differ by polar group, length of fatty acid chain and degree of saturation  affects the fluidity of the chain o important for biological membranes  b/c they are amphipatric molecules (have both hydrophobic and hydrophilic portions)  allowing for critical properties of life. o If they are put in H2O; spontaneously assemble to minimize the hydrophobic interaction w/ H2O  Can form micelles  In majority causes though, end w/ phospholipid bilayer (which seals up)  basis of all membranes Waxes – long chain fatty acid + long chain fatty alcohol or carbon rings  Form soft solid masses  Water proof coatings on leaves, bark, fruits, feathers  Structural material in beehives  Protective coating in ear canal Lipids w/o fatty acids  Sterols – 4 fused carbon rings + various functional Groups o In animal cells  Buffer of fluidity  Hormones (ex. Testosertone)  Vitamins Proteins  Many functions: enzyme, structural, transport, motor, storage, signal, receptor, gene, regulatory etc. o Enzyme: catalyzes formation or breaking of bonding o Structural: cytoskeleton; form hair, nails o Transport: hemoglobin  heme group transports oxygen o Motor: act in filaments – densely packed in muscle cell w/ myosin, allows for contraction. o Storage: proteins bind to small molecules and store it o Signaling: turns on and off processes.  Ex) cAMP  can phosphorylate molecule to turn on and off o Receptor: insulin binds to receptor protein  signal needs  regulate amount of insulin in blood otherwise stores o Gene reg: certain proteins turn on others turn off  If work is to be done in a cell, almost always uses proteins.  What are they? o Unbranched chain of amino acids (subunit) o Linked by peptide bonds  allows for stabilize 2 ndand 3 structure o Variable size (30 – 10,000 amino acids)  Subunit Amino acids  Our bodies can digest 11 Amino acids, need metabolites to digest 9 form food  20 amino acids  side chain determine structure of protein Peptide bond = carboxylic acid (aa#1) + amino group (aa#2)  2 terminals don’t combine b/c w/o enzyme to link chain, won’t occur spontaneously in time frame that is relevant to life  Dehydration synthesis occurs  Polypeptide: chain of amino acid (not necessarily in final 30 structure form) Protein has assumed final functional folding structure may be composed if 1 or more polypeptide chains.  Protein Structures o Stable and unique for each protein o Specified by amino acid sequence  And properties by R groups Structure of each protein  drives function  Every protein has its own unique structure and conformation o Amino acid sequence specifies the function  based on the chemical properties of the side chain.  Noncovalent interactions (individually weak, together makes structure stronger o Electrostatic attraction b/w ions o Vander-walls: momentary dipole by redistribution of e- clouds of adjacent molecules o Hydrophobic interactions: drive up side chains to core to minimize interaction w/ polar molecules  This helps maintain 30 shapes  Non polar interactions  Disulfide bonds stabilize some extracellular protein structures o 2 cysteine molecules covalently bond to form disulfide bond Hierarchy of Structure (protein)  Linear order (Primary Structure) o Sequence of amino acids o No folding o Predicted form CDNA sequence o Determines how protein will fold  ultimately func.  Secondary structure o Forms Alpha-helix or β – pleated sheet o H bonds in the backbone which maintains its structure w/o interacting with side chains  Thus b/c no interactions w/ side chains, many many dif proteins can form this structure as w/ all proteins have the same backbone  Sometimes they don’t form when it doesnot fit the shape of the structure  Tertiary Structure  3D conformation of polypeptide o Folding of the 2ndstructure  This occurs dure to side chains  mainly from electrostatic attraction. o Some proteins stop here are fully functional  Quaternary Structure o Folding β – 3D conformation of more than one polypeptide  Homodimer = same polypeptide  Hetero = dif.


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