Biology 107 week 1 notes
Biology 107 week 1 notes Bio107
Washington State University Vancouver
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This 10 page Class Notes was uploaded by Lorina Tomceac on Tuesday February 10, 2015. The Class Notes belongs to Bio107 at Washington State University Vancouver taught by Dr. Michel Berger in Fall. Since its upload, it has received 213 views. For similar materials see biology in Science at Washington State University Vancouver.
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Date Created: 02/10/15
Bio 107 Lecture 1 Bio 354 Human anatomy ad before wsu login for the video rst quiz due next Tuesday 10 AM Register iclicker WSUV network id Protein denaturation unraveling of proteins and become dysfunctional Molecules are made up of monomers Monomers put together form polymers Polymer gt Example amylase l starch VVVV 3 O Dehydration reaction lts enzyme mediated reactions Enzymes split a hydroxyl group OH from one monomer and H from another A covalent bond forms between two monomers Water is the byproduct in this reaction Hydrolisis reaction 0 A polymer is split into two smaller molecules 0 Reverse reaction of dehydration An enzyme adds water and splits a molecule Carbohydrates sugars monosachridel one monomer Disacharide two monomers Polysacharidel many monomers Aldose or keytose is determined by the location of the carbonyl group aldose l where the C O is terminal keytose the CO is somewhere in between Biology 107 lecture 2 notes 011515 Review chapters 24 and read chapter 6 Review the writing assignment Polysaccharides long chains of carbohydrates 0 Different glycolsidic linkages result in different 3D structures 0 Parallel cellulose polymers hydrogen bonds between hydroxyl groups attached to carbon 393 High fructose corn syrup VVVV VV Corn starch amylose polysaccharide The way you produce glucose from amylose is by using a hydrolysis reaction to split apart the polymer Industrial hydrolization of corn starch into glucose monomer To convert glucose syrup to fructose syrup you would have to convert an aldose to a ketose by rearranging position of carbonyl group Enzymatic reaction used to rearrange atoms of glucose into fructose High fructose corn syrup 55 fructose and 45 glucose Glycogen gt gt gt gt Glucose polymer Used in animals to store energy stored in high concentration in liver tissue and muscle tissue Blood sugar is the concentration of glucose drop in blood sugar Glycogen can hydrolyzed into glucose monomers as a temporary source of energy Lipids gt gt not true polumers hydrophobic not soluable in water constructed from glycerol glycerol alcohol with 3 carbons Three fatty avid molecules are bound by a dehydration reaction Ester linkage is formed between hydroxylOH and carboxyl COOH 39 Saturated only single bonds very linear solid at room temperature Most animal fats I Unsaturated one or more double bonds liquid at room temperature plant fats the double bond makes it more reactive and easier to break down trans fat unsaturated fat with a trans double bond function of lipids 39 Storage of energy Two times as much energy per gram in lipids compared to carbohydrates O 90 O 90 I Insulation 39 Cushioning Phospholipids gt Cell membranes composed mainly of phospholipids gt Two fatty acids attached to glycerol gt Third fatty acid replaced with a negatively charges phosphate group 0 Hydrophilic head and hydrophobic tale so that it can easily bond to water 0 Allows things to be soluble inside and outside the cell 0 Regulates what enters and exits the cell Steroids gt Cholesterol gt Precursor for other steroid synthesis gt Testosterone and estrogen Proteins gt Diverse functional molecules gt 50 of dry weight of cell gt Enzymes amylase or sucrose Different functions 39 Structural keratin finger nail I Hormonal insulin signaling molecule 39 Storage ovalbumiun egg white Proteins are formed from amino acid monomers 20 amino acids used to produce proteins should probably memorize themsee Fig 514 VV V Formed of 1 amino group amino end Nterminus l carboxyl group carboxyl end Cterminus and 1 R group R can be different for each amino acid A dehydration reaction links carboxyl group to amino Forms a peptide chain polypeptide Polypeptide undergoes further structural changes Each protein has a unique structure and function Protein structures 1 Primary structure unique sequence of amino acids helix 2 Secondary structure hydrogen bonds in the backbone coil and fold protein 3 Tertiary structure protein loops bends and folds on itself Hydrophobic regions interact Disulfide bridge covalent bond between two cysteine monomers with sulfhydryl groups Becomes functional 4 Quaternary structure aggregation of multiple sub units Specific sequence of amino acids is what makes the proteins specific It changes the function and meaning of the protein A mistake in protein formation can make a protein nonfunctional ie sickle cell anemia substitution of one amino acidO DNA mutation results in the exchange of one single amino acid A hydrophobic region of one subunit becomes exposed Red blood cells containing the mutated protein shape becomes distorted VVVV VVVVVV Protein denaturation VVV Unraveling of a protein into a nonnative shape Improper pH salt concentration temperature or other environmental factor Denature egg Whites Proteins can renatured after environment returns to normal and be put back into function Molecular chaperons chaperonins I Protect the protein While it folds I Exposed hydrophobic regions can form aggregations Which are toxic Nucleic acids gt gt gt Store and transmit basic genetic information Deoxyribonucleic acids I Double stranded With hydrogen bonds holding the strands together Ribonucleic acid RNA I Single stranded I Transcription synthesis of mRNA in the nucleus I Translation synthesis of proteins What nucleic acids are I Chains of repeating nucleotides I Simple 5 carbon carbohydrate joined to phosphorous and nitrogen containing molecule I DNA deoxyribose no oxygen on second carbon I RNA ribose 5 and 3 I 4 bases adenine guanine cytosine and thymine DNA and uracil RNA I purines larger compared to pyrimidines I monomers are linked together by a phosphate group Base paring rules 0 A pairs With T in DNA or U in RNA I G pairs With C DNA sugar phosphate backbone are external I Nitrogenous base internal I Strands in opposite 3 to 5 direction Biology 107 Lecture 3 Chapter 6 Cells oz Cells gt a cell is the smallest living unit gt Range from 1 micrometer to 100 micrometer gt Area is proportional to linear dimension gt Materials must be able to ef ciently move in and out of cell oz Prokaryotic cells gt Bacteria and archaea gt Small and simple gt Don t have a membrane bound nucleus gt Don t have organelles oz Eukaryotic cells 0 90 gt More complex and intricate compared to prokaryotic cells gt Have a membrane bound nucleus gt Complex organelles Internal compartments Prokaryotic cell structure gt Have agella used for locomotion gt Capsule gellike polysaccharide used for protection and attachments Fimbriae used for attachment Plasma membrane transportation in and out communication receptors Cell wall structural support maintain cell shape Ribosomes synthesize proteins Nucleoid region where DNA is located Bacterial chromosomes DNA ukaryotic cell structure Review g 68 Nucleus Contains and separates the genetic material DNA from the cytoplasm Double membrane phospholipid bilayer Nuclear pores regulate entry and exit molecules Nuclear lamina protein laments that provide structural support Chromatin aggregation of chromosomes when cell is not dividing Nucleolus most obvious structure synthesis of ribosomal RNA large and small subunits gt Ribosomes Responsible for protein synthesis VV IT39VVVV gt gt gtEn gtGo Assemble protein from genetic instructions mRNA Two types 9 Free in cytoplasm 9 Bound to endoplasmic reticulum ER or nuclear membrane doplasmic Reticulum ER Network of membranes tubules and sacs cisternae Continuous with nuclear membrane Smooth ER 9 Synthesis of lipid oils phospholipids amp steroids 9 Storage of calcium ions important for cell communication Detoxi cation of drugs amp poisons ex Alcohol being detoxi ed gt Addition of hydroxyl group gt Proportion can increase or decrease high abundance of cells need higher proportion to have the same effect gt Can modify the abundance or ER Rough ER 9 Synthesis of secretory proteins o Transport vesicles quotbudquot from transitional ER region 9 Produces membranes for the cell 9 Site where membrane material is produced lgi apparatus Receiving storing and shipping center Cis face quotreceivingquot region Trans face shipping region Cisternal maturation model Cisternae move from cis to trans face Molecules are modi ed as cisternae move Molecular tags speci c to destination can be added O gt Lysosomes Membrane enclosed bag of hydrolytic enzymes Low pH in lysosomes Lysosomal enzymes do not function in neutral pH of cytosol Mechanism for intracellular digestion Phagocytosis engul ng of particles Autophagy gt Vacuoles Membrane bound vesicles Food vacuoles Contractile vacuoles Water regulation in protists Used to pump water out of cell 0 Used effectively as pump Central vacuole Plants 9 Storage of macromolecules and inorganic ions gt PROTEINS gt K and Cl39 gt Pigments gt Secondary metabolism Mitochondria Amoeba plant animals and fungi have it Can be really abundant hundreds to thousands per cell Site of cellular respiration Converts energy for cellular use Produces ATP Semiautonomous organelle Contain a small amount of DAN Grow and reproduce within the cell Two membranes 0 Smooth outer membrane Convoluted inner membrane increases surface area to volume ratio Mitochondrial matrix region enclosed by inner membrane Chloroplasts Site of photosynthesis Semiautonomous organelle that contains DNA Contain chlorophyll green photosynthetic pigment Two membranes inner outer membrane lntermembrane space Stroma uid lled region outside of thylakoids Thylakoid inner membrane structures Peroxisomes Membrane bound compartments 0 Contain enzymes that transfer hydrogen to oxygen H202 product 0 H202 is converted to water by enzymes 0 Breakdown of fatty acids for respiration o EtOH detoxi cation Cytoskeleton Network of three types of bers microtubules thick micro laments thin and intermediate laments midsized Mechanical support Organelle anchorage Cell mobility with aid of motor proteins Microtubules o Hollow rods composed of tubulin o Tubulinpolypeptide dimer alpha or beta dimer form a cyHnd calshape Tubulin can be added or removed Cell mobility cilia or agella bundles of microtubules Chromosome movement during cell division Organelle movement Motor proteins carrying a vesicle walks down the microtubule by using ATP 0000 Cilia and agella Used by cells for locomotion or movement o Microtubules drive the movement in cilia and agella Microtubules used to beat agella and cilia Flagella Undulates One or a few per cell 0 Relative long 10200 micrometers compared to cilia Cilia 0 Back and forth motions Occur in large number on cell surface Relatively short 220 Mm compared to agella o Motile or non motile cilia Cilia and agella Ultrastructure similar between agella and cilia core of microtubules sheathed in an extension of the cell membrane 0 92 pattern nine doublets of microtubules in a ring ans two single microtubules in the center 0 90 pattern for nonmotile cilia Microtubules assembly anchored by a basal plate Crosslinking proteins connected doublets Neighboring doublets also anchored Dynein motor proteins responsible for bending of microtubules ATP changes shape of protein Dynein foot releases and reattaches one step further along the microtubule o Flagella o Wavelike motion produced by synchronized movement of dyneins o Movement from base to tip Chromosomes movement during cell division Microtubule formation initiated Micro laments 9 Twisted chains of actin subunits Network of micro laments support cell shape Cell motility Microvilli have core of micro laments Muscle cell contractile apparatus gt Actin laments arranged parallel within muscle cells gt Interact with thicker protein laments myosin o Myosin is a motor protein 9 Actin and myosin slide past each other 9 Shortens the muscle cells Amoeboid movement o Interaction between actin and myosin 00 393 Intermediate laments gt Diverse class of cytoskeletal elements gt Constructed from different molecular subunits gt More permanent compared to microtubules and micro laments gt Reinforce cell shape gt Hold positions of organelles Plant cell wall gt Extracellular structure gt Protection gt Suppo Primary cell wall Cellulose is secreted into the extracellular space 0 Embedded into matrix of other polysaccharides and proteins 0 Between primary cell walls in the middle of lamella Pectin Glues adjacent cells together Secondary cell wall 0 Between plasma membrane and 1 cell wall can be secreted 393 Animal extracellular matrix ECM gt Glycoproteins secreted by cell gt Collagen gt Fibronectin bind to cell surface receptors Used for cell communication ntraceuarjunctions gt Plants Plasmodesmata o Perforated channels lined with plasma membrane Allows water and small solutes to pass between cells gt Animal ces Tight junctions 0 Plasma membrane are tightly bound together by proteins 0 Prevent leakage of extracellular uid 0 Common in epithelial cells 0 Limits uid moement Desmosomes Fasten ces together 0 Attach muscle cells together in a muscle Gap junctions Cytoplasmic channels 0 Used for communication 0 Small molecules can through
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