University:
Marymont University
Course:
BIO 110 | Introduction to Environmental Science
Academic year:

2023
Views:

303

Pages:

17
Author:

Athena Harrison

Carbohydrates Structural: • Cellulose : found in plant cell walls • Chitin: found in fungi cell walls & Composed of C, H, & 0 - Ratio: 1:2:1 Monomer: Monosaccharide Glucose H C1 H C-0 I Storage: 0H \I • • C l'\9 HO �/ I C--C � 6H Monomer: Amino Acid Hydrogen exoskeleton of arthropods CH,OH H Proteins Composed of C, H, 0, N, & S H Amino Starch: found in plants Glycogen: found in animals Starch vs. Cellulose Examples: Glucose, Fructose, Galactose R group Disaccharides: Two monosaccharides Bond: Glycosidic Linkage Examples: Sucrose, Lactose, Maltose R �roup 1-fy.lrc·pillllo Bond: Peptide bond (between carboxyl & amino groups) N terminus Fold F"1:erior l"tu1or F"1:erior 1-----1-------1 Quaternary : • Bond: ANY (hydrogen, covalent, Ionic, ... ) between R groups of different polypeptides flph l,oncl C terminus Nucleic Acids 5'end Composed of C, H, 0, N, & P Lipids Purine: Double Ring • A&G Phosphate �'"0"6 """" H03' Directionality: 5' -$. ➔ 3'; antiparallel Phosphate A& T 2 3'end C&G 3 DNA RNA A, T, C, G A,U,C,G Sugar 0eoxyriboe;e Ribose Strandl:dnu6 "double� "single" Hydrophilic head Attracted to water Glycerol H t,on...16 Nltrogenou6 Ba6e6 Phospholipids Fats Ba� Pairing Bond: Phosphodiester linkage (between phosphate and hydroxyl) All of the lipids are NON POLAR!! Monomer: N/A Pyrimidine: • Single Ring • C. U, T Pentose Sugar \_Jr Composed of C, H, 0, & P (in phospholipids) Nitrogenous Bases Monomer: Nucleotide x-K::�\ ."x;0 11 . � K-�� Leveli:, of Protein Structure: Primary: • Bond: peptide bonds between amino acide, • Structure: string of amino acide, Secondary: • Bond: hydrogen bonds between backbone • Structure: alpha helix or beta pleated sheet Tertiary: • Bond: ANY (hydrogen, covalent, ionic, ... ) between R groups • Structure: final 3D structure Hydrophobic ta II Repelled by waler 2 fatty acids • • . ..,,.. .......... Amphipathic Interstitial Fluid (Extracellular) Saturated fatty acid • ALL single bonds • Each carfJon is SATURATED by hydrogen Unsaturated fatty acid • At lea&t one double bond • Not all carbon& are SATURATED by hydrogen Cytosolic Fluid (Intracellular) Steroids o5° General structure Four fused rings Ligand: • Intracellular Reception Polar Polar covalent bonde; between oxygen & hydrogen p-.Jropm - "sutface" based on the interaction of hydrogen bonds Allows you to skip rocks or wate st-riders to walk on wate Less Dense when Solid Hydrogen bonde; inhibit compaction Ice floati:;; temperature buffe High Specific Heat Water must absorb or release A LARGE amount of energy to change 1 gram of water by 1 ° c. Evaporative Cooling Release water on surface of organism to absorb heat energy from body (and break the bonds cooling down the organism) pH=� log [H4] •� ,= lee Kydrogi'.n bon blo con Temperature Buffer • • Coastal Regions Body Temperature gt! Ai:; the concentration of hydronium/hydroge ion increases, the pH decreae;es -- Nucleus Structure: • Double membrane (nuclear envelope) with pore5 unctions: • Stores genetic information (DNA) • Synthesi5 of RNA • Ribo5ome 5ubunit a55embly Rough ER Smooth ER Structure: • Membrane studded with ribosomes attached to nuclear envelope FunctioM: • Site of membrane-bound protein and secreted protein synthMi5 • Cell compartmentalization • Mechanical 5upport • Role in intracellular tran5pOrt Structure: • Folded, tubelike structure (cisternae) Functions: • Detoxification • Calcium Storage • Lipid synthesis Cellular Organelles Structure: • Compoe;ed of rRNA and protein • Large & ;;mall eubunite; • Type;;: bound or free (cytoplae;mic) Structure: • Membrane-bound structure comp05ed on flattened sacs (ci5ternae) Functions: • Folding and chemical modification of functions: • Protein synthesis synthesized proteins • Packaging protein traffic Ribosomes Golg i Complex Lysosome Mitochondria Structure: • Double membrane (outer. smooth; inner. highly folded) functions: • Site of oxidative phosphorylation (crlstae/lnner membrane) • Site of Krebs Cycle (mat-rix) Structure: • membrane-1::ncloE?ed E?.SlCfi that contain hydrolytic t::nzymeE> functione: • Intracellular digestion (recycle cell organic materials & programmed cell death: apoptosis) Cellular Organelles Structure: • membrane-bound sac functions: • storage and release of macromolecuiles and cellular waste products • Central: water retention - turgor pressure • Contractile: osmoregulation (protist) • Food: phagocytosis, fuse with lysosome Nfllllll'MI Structure: • Double outer membrane (thylakoio sac stacked: grana ano fluio: stroma) Functions: • Site of photosynthesis • Thylakoid: Light Reactions • Stroma: Calvin-Benson Cycle Chloroplast Vacuole s,urface Area: Volume Volume: V = j 1t Surface Area: S = H 4xr2 Volume: V = s 3 Surface Area: S = 6s2 h Volume: v. LWH Surface Area: S = 2LH + 2LW+ 2 Volume: V = 1[ r2 h or V = Bh Surface Area: S = 2x.r2 + lxrh s d Plasma Membrane Compo5ed of: • Phospholipids • Membrane Protein5 • Glycolipids/Glycoprotein5 Cholesterol • Facilitated Diffusion Simple Diffusion • • • • • • Active Transport • Pa55ive Tran5port, No NRG • Down concentration gradient • Small Molecules • Requires transport protein Channel v5. Carrier protein • Example: water, Na+ , K + , ca• Pa55ive Tran5port, No NRG Down concentration gradient Small, Nonpolar No tran5port protein needed Example5: CO 2 , 0 2 , N2 , 5teroid5 Small amount of H 2 0 leak through membrane • • • Require5 input of NRG Against concentration 13rndient Require5 tran5port protein (carrier protein) Example: Na+ . K... , Ca + , W • Membrane Transport • • • • Bulk Transport. Endocytosis Import of materials Phagocytoe;is: Cellular Eating -·Pinocytoe;is: Cellular Drinking • Receptor-Mediated: Endocytosie; =... "' number of water molecules• 24 number of solute molecules• 0 number of solute molecules • 5 "' number of fr•• water molecules • 24 *"' cj + cj number of fr•• water molecules• 4 HIGH solute concentration LOW free water concentration • GAINS water from hypotonic 5olution • • • • • • • • • •• • • • • • • --• • D D • • • □-·••:· • • ••• ••••• ---+ • • □O: □ •••••• ••• HIGK WAllR lo.-J WAllR fDHNIIAl fDHNIIAl EQUAL solute concentration (as other i:;olution) EQUAL free water concentration (ai:; other solution) • .... ••ti•• ,. • • • .••• o.• □ • • • •• □ • • □•••••• •□ •• ••••• •□ •• • WAl[R MOO[S � OSMOSIS fROO\ HIGH IO lo.-J WAl[R fDHNIIAl Hypotonic Solution • • LOW solute concentration HIGH free water concentration LOSES water to hypertonic solution Equal water movement into and out of solution Osmosis .. ,� • • D D D D Isotonic Solution • • -- • 1Ml • PlRMlABl[ M[MBRAN[ � Hypertonic Solution • •• . . . ·•·.-.·.•.··:" � mimber or water molecules• 24 � � � 4-, ci � ci � � � � � � � � 4? ci � ci 4? � � � � � � Export of materials Rough ER (synthe5ize) ➔ Golgi complex (package/modification) ➔ Pla5ma Meml;>rane • Hi9h solute concentr•tlon Low solute concentration Exocytosis .. Endergonic Reaction • • • ENDEAOONIC R£ACTIOH.. 40 > 0 Enzymes D.t:RGOMIC Rr.ACTlON� 6G < 0 Not e;pontaneoue; ABSORB energy Example: ADP + P1 • • • ➔ ATP Spontaneous RELEASE energy Example: ATP ➔ ADP + P, • • • ._ enzyme changes shllj)e Functions slightly as subsuare binds Biological catalyst Speeds up chemical reactions Reduces the activation energy --+ Exergonic Reaction (DStae Starting Material: -� r.-mr.• j .. t Chain Electron Traner>or If .. ., FNADH/FADH 2 (electrons) -.,.,,,Y,,.,,Y""-Y.,..-.,...,. • Protons pumpc:d into IM sp,;ice """-':xJr"itb:X"tOcr-�r-: v�v.___;1._ry':!II!...�..,....., • Product: • Generates proton gradient ATPs • Fin;;1I electron ;;1cceptor: OXYGEN • Two Parts: Electron Transport Chain & Chemiosmosis • • of Ille enzym Photosynthesis Krebs Cycle Location: Mitochondrial Matrix Staring Material: Acet;yl CoA Pr oducU: 0 Ille Products leave �CIJ..e lie Competitive: • Binds to active si Noncompetitive: • Binds to allosteric site R..acllon Progress Cellular Respiration Glycolysis (vSUbstralA! Is convened to products. Inhibitors What is Gibbs Free Energy? • Enzyme/subslrnt (!) complex k>rms. Electron Trane;port Chai 1-r tt � • Protone; are pumped into the thylakoid space • • Calvin Cycle Location: Stroma Starting Material: 3 CO 2 9ATP 6 NADPH ic Reaction EHD£AOOMC REACTlOfrt. UJ > 0 • • • txtRGOollC RtACTION: aG < 0 RMc:ttoni•�· 1------- Not spontaneous ABSORB energy Example: ADP + P 1 ➔ ATP • • • g it j SpontaneouG RELEASE energy Example: A fP ➔ ADP + P 1 1 nrno Exergonic Reaction Tlmo Grbbs Fr,ee Energy & Reactions What is Gibbs Free Energy? • LLlG = LlH - TLlS_J I r . Functions • • • I J LlG = LlGt - LlGi Enzymes enzyme changes ,;h sllghdy as subsua1e binds products Biological ca-talyGt Speeds up chemical reactionG Reduces the activation eneri:iv ■■ ■ Q) SUbslrate • erners aclive site ol enzyme. .0 .0 Reaction Pr09reu • • • Energy available to do wor Important Notes: Enzymes are PROTEINS Are NOT consumed by the reaction Have no effect on the change in Gibbs Free Energy -+ ■■ ■• --+ Q) Enzyme/substt�te complex lorms. Competitive: • Binds to active site Noncompetitive: • Binds to alloe;teric site Denaturation -+ @Sd>strall! 15 convened to product�. hibitors Environmental Temperatures pH (outside of optimal range) Salinity © Products leave Ille aetwe sue or Ille enzy!l1e. camu ,.,,,eiro, \ ® �' w tQ-J-{0�\PffilM N'lelkJft Cellular Respiration Glycolysis • • • Krebs Cycle • • Location: CytoGol Starting Material: Gluco5c Products: 2 Pyruvatc 2 NADH 2ATP • Location: itochondrial Matrix Staring Material: Acetyl CoA Proaucts: 2C0 2 3NADH 1 FADH 2 1ATP Oxidative Phosphorylation • • Location: MitochonJrial Cristae Starting Material: Electron Trane;.port Chain NADH/FADH 2 (electrons) • Protons pumped into IM sp,;ice "-'�nlCTY.:"'{X��-X,,""'x,.'"X,.')..:)..,_r-"-r-"r.,._-v J..��'"""' • Product: • Gener,;ites proton gradient ATPs • Ffn,;il electron ,;icc;;eptor: OXY'GE.N • Two PartB: Electron Transport Chain & Cnemiosmosis Photosynthesis Light Reactions • • • Location: Thylakoid Membrane Starting Material: Water (electrons) Photom, (energy) Products: _.-::,,,oo,i_...._ ATP • • Unear Electron Flow PS I & PS 11 Syntl1esizes ATP & NADPH Cycl'c E e:ctron Flow • PS I ONLY • • • Calvin Cycle Location: Stroma Starting Material: 3C0 2 9ATP 6 NADPH Products: G3·P -y-/:�---,,.-,_ �( lfJJ "LO,•i1t· tr Electron Trarisport Chai!n ir tr tr • ProtonE? are pumped into the thy1akoid space -�· "' :. Cellular Communication Reception Response Transduction Ligand (sig,naling molecule) 17inds to receptor Ca uses con-Fi rmationaI shape change Ex: G protein coupled receptor Signaling cascades relay signals from receptors to cell targets, often amplifying the incoming signals Sterofd Hormone Phosphorylation Cascade Release: Simple Diffusion Receptor: Intracellular Exam1?le: Testosterone, Estrogen Protein Kinae;e Phoe;phorylate relay molecule:e; Protein Hormone Secondary Messengen, Release: E.xocytosis Receptor: Extracellular Example: Insulin Ca 2+ cAMP cell growth secretion of molecu[es gene expression apoptosis Cel:lular Communication _ ,1r.iccllul:i u,d ( N"clcu, )'IOplu,m /1 Transduction �l� 0 �""""'� �ma Mcmbrune Parent Cell Ploidy Mitosrs Meiosis Respo Diploid Diploid Rounds of DNA Replication 1 1 \ Rounds of Daughter Cell Nucfear Ploidy Division Diploid 1 Haploid 2 Mitosis vs. Meiosis Compare to Parent Cell Crossing Over Independent Assortment Mitosis Identical Meiosis Genetically Distinct Does not occur Occurs in Prophase I Does not occur Occurs in Metaphase I Number of Daughter Cells 2 4 s G, The cell grows through all the different phases of interphase Duplication of cell organelles Sy thesis of proteins. R A. and building blocks Replication of genetic material and centrosomes I nterpha se 5ynthee;ie; of proteins and R A a es organelles Reorganizes cellular conte t6 c� I Cvcle PREPARE to divide M PW1¥15! Sister Chromatids pulled ite poles APART I) MUM Sister Chromatids line up in the MIDDLE �PAA� Division of the cytoplasm (ID Cytokinesis ® IHGrnAS! TWO new uclei are formed e plate INDEPENDENT ASSORTMENT Anaphase I HOMOLOGOUS CHROMOSOMES separate to opposite poles Meiosis (IIJJf..lMl/1. A Nuclear envelope forms around the HAPLOID .daughter cells Meiosis I iotr'o ogous Chrori1osomes 'v1eios s I S ster Chrori1t, ds lllliltOW!l> OIKIINIDlli� Will fRltll ({Nl!J�')JtJ Cf i'Jllll5 Chromatin condenses Sister cnromatids align Prophase II Telophase I SISTER CHROMATIDS align SISTER CHROMATIDS 011 the metaphase plate separate to opposite poles Metaphase JI Anaphase JI Nuclear enve[ope forms around the HAPLOID d.aug,hter cells Telophase I Inheritance Patterns Complete Dominance Monohybrid Homozygou5 domi11ant and heterozygou5 look the Game I Codominance Heterozygou5 i5 both domfnant trait5 i11 organie.m y yy y Yy y Yy yy R r R RR Rr r Rr rr lncomplete Dominance Heterozygous is a blend betwee,n the tw'o dominant traite; B B C C Y Y C C YI Heterozygous for ONE traft Yellow: 3/4 Green:¼ Round: 3/4 Wrinkled:¼ Yellow & Round::¾ x :¾ = 9/16 Yellow & Wrinkled: 3/4 x ¼ = 3/1-6 Green & Round: ¼ x 3/4 = 3/16 Green & Wrinkled:¼ x ¼ = 1/16 8 CC Complete Dominance: 3:1 ratio Incomplete or Cadominance: 1:2:1 Dihybrid Heterozygou5 for TWO trait5 Complete Dominance: 9:3:3:1 ratio Incomplete or Codominance: 6:3:3:2:1:1 Inheritance Patterns Autosomal Inheritance Allele ie; locatt:a on an auto·Bome (non-Bex chromoe;ome) Sex-Linked Allele ie located on a e.ex chromoe.ome Materna[ Inheritance Autosamal Recessive ] Allele ie; locatt:a on the DNA fauna in a mitochonarial or .--�-.-------, chloroplast ( Sex-Linked Recessive ] Linked Genes Genes loc;;;ited on the 6;;;ime chromosome clo6ely together Autosoma I Dominant Central Dogma replication DNA ➔ R> A ➔ Polypeptide > 1 1 transcrit:tion translation Replication PRDtAl!Y01i£ Location Replicatiorn FOfk Eut:AKYOIE • Euka ryote5: nui:;leu5 .... DNAS.'/lllheslw • Prokaryote5: nucleoid 5"tn �' �· V fi' r�::r:.��lir.,ti(lll Structure J • Eukaryote5: m ltiple line.ar • 'sJ".i> � 0 ;;.;-© 6 � , r,i....,. .. cm..,, a � .. • Proka ryote5: single circular "% �,.::; Eu™E · � Import.ant- EnzymeG :=�;mu,SE � • HelicaGe unwinds tne DNA G-trancfo riw.,.-.c �:r· ' )€):r �� . . . . CW. l'OlYMEIUl!lE RIP1'GOMEIUl5E • Topo1GomeraGe relaxes superco1l1ng 1, iW.pol ,a ""' t:l!Af"L6 front of tne replication fork. 1vw.J>d., (� . • • Prlmase syntnesizes the RNA primer ow,p,1.a: !i (DNA polymeraGe requires RNA primers to init�ate DNA synthesis). • DNA polymerase synthesizeG new GtrandG of DNA continuously on the leading Gtrand and discontinuously on tne lagging strand. • Ligase Joins the fragments on the lagging Gtrand. ��:! .,, �� V/� �:�..z, Transcript ion Reminders about DNA: • DNA made up of: - nitrogenous base (A, T, C, G) - pentose sugar (deoxyribose) - phosphate group • Purine (A/G) have a double ring structure • Pyrimidine (CIT) have a single ring stn.Jcture • Base Pair Rules • A & T with 2 H bonds - C & G i,,lith 3 H bonds • Sideedness - 5' end: phosphate • 3' end: hydroxyl group • Directionality - Read 3' to 5' - Synthesize 5' to 3' (Remember ANTIF'ARALLEL) frmplau: Strand ( non,::;od iri� t>tr�rid. minut> otrand, or antiuml' t>tr�rid) Location Important Enzyme & Components • Eukaryotes: nucleuG • RNA polymerase synthesizes mRNA molecules in the 5' • Prokaryotes: nucleoid (cytosol) to 3' direction by reading the template DNA strand in R6minders about RNA: the 3' to 5' direction. • DNA made up of: • Promoter: site where RNA polymerase blnds to start - nitrogenou5 base (A, U, C, G) transcription - pentoM sugar (ribo5e) • Transcription Factors: activators/inhibitors to turt1 - phoe.phate group on/off gene expression • Purine (A/G) have a double ring e.tructure • Pyrimidine (C/U) haw� a e.ingle ring e.tructur� • Bae.e Pair Rules - A & T(DNA)/U(RNA) l.vith 2 H bonde. - C & G with 3 H bonde. • Sidenee.e.es 5' - 5' end: phoe.phate z Nudeoll degradation from hydrolytii:; enzyme5 in cyto5ol 5' Guanine Cap • SignalB the "start" of the mRNA transcript for ribooome to bind • Facilitates- export from nui:;leus- J� s� .J � � �11 ) · t · t J D. •I _ U; ,D. Splicing • Remova I of intronB from pre·mRNA trane;cr ipt r� :J Q ·5• Transla·tion 51.1l'unlr W1n,h rRNA,1 tRI Small Suruni (blnJ!' mt-�N.-\:, IRM ·�'{/' Location • Eukaryotes: cytosollrough ER • Prokaryotes: cytosol Stevs of Translation • Initiation: start codon (AUG) • Elongation: vase pair between tRNA/mRNA with amino acid added • Termination: stop codon (UAG. UAA, UGA) Mutations Point Mutations Mutation at one nucleotide vase pair � no change in amino acid (AA) Missense change from one AA to another AA Frameshi� insertion/deletion of 1 or 2 nucleotide base pairs shifts the reading frame fo codoM Noneyenpe change from AA to STOP codon ORIGINAL DNA: ml!lll:otltti4i.lf'W10ilddliwCIM _ .I ··- Ch romosoma I Mutations Rearrangement of chromoe;ome parte:; or changee; in chromosome number5 Rearra naement lne;ertion Deletion Duplication Inversion Transloc8tion Chanees in Chromosome Number Nondisjunction PolyPloidy Operons Gene Regulation found in prokaryoteg, Fromoter Site when RNA polymerase binds Genes DNA Operator ·Site when repressor binds Repressible Operon Inducible Operon Example: Trp Operon Gynthesizes trypt.ophan Example: Lac Operon synthesizes enzymes to break down lactose StartG: ON Repressor: INACTIVE Starts: OFF Represso r: ACTIVE If trp is present.,. lrp binds to repressor to ACTI\/ A TE Repressor binds to operator to turn the operon OFF If lactose is present ... lactose binds to repressor to IN AC111VA TE Repressor no longer binds to operator to tum the operon ON Gel Electrophoresis Separate molecules based on size and cnarge L Polymerase Chain Reaction (PCR) Make.z; multiple copie.z, of DNA fragments � 1. Heating 2, Cooling, 3. Annealf ng; BioT ech no logy r Bacteria I ra nsformation Introduce genetic ma1terial (plasmid) to bacteria1 DNA Sequencing Use radioactive nucleotides to determine the e;equence of a DNA strand ,#: . .. . 0 L, I' 0 ctJQ/IIIHlll>III - @ ..,.NIN', , r ; �/,, .,' nnnnrnO (II ............ �"'-"""' Iii lltlll.ii.liilli�IIL.0 111111 jjl!li 11,111 1D iiiiil ihiii]iii. nn! • � ,:- I • t I , lriN,1�J .. " Q