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| 8075999973 | Macromolecules | smaller organic molecules join together to form larger molecules | 0 | |
| 8076035016 | 4 major macromolecule classes | carbohydrates, lipids, proteins, nucleic acids | 1 | |
| 8076035017 | Polymers | longer molecules built by linking repeating building blocks in a chain - many monomer | 2 | |
| 8076077881 | Dehydration Synthesis | - joins monomers by "taking" H2O out - one monomer donates OH- - other monomer donates H+ - together these form H2O - Condensation reaction |  | 3 |
| 8076094535 | Digestion/ Hydrolysis | - use H2O to breakdown polymers - revers of dehydration synthesis - cleave off on monomer at a time - H2O is split into H+ and OH attach to ends |  | 4 |
| 8076115912 | Carbohydrates | - carbohydrates are composed of C,H,O | 5 | |
| 8076126300 | Carbohydrates Function | - Energy --> ATP - Energy storage - raw materials - structural materials: cyton, cellulose | 6 | |
| 8076137524 | monomer of Carbohydrates | sugar | 7 | |
| 8076139555 | Sugars | - most end in -ose - classified by number of carbons | 8 | |
| 8076142258 | Monosaccharides | - simple 1 monomer sugars - glucose | 9 | |
| 8076146085 | Disaccharides | - 2 monomer sugars - sucrose | 10 | |
| 8076149122 | Polysaccharides | - polymers of sugar - cost little energy to burn | 11 | |
| 8076165575 | Function of sugars | - energy storage - starch, glycogen | 12 | |
| 8076172399 | Linear polysaccharides | starch - easy to digest | 13 | |
| 8076176545 | Branched polysaccharides | - Glycogen - hard to digest | 14 | |
| 8076192452 | Cellulose | - most abundant organic compound on Earth - herbivores have envolved mechanism to digest i - most carnivores can not digest it | 15 | |
| 8076200136 | Proteins | - structurally and functionally diverse | 16 | |
| 8076217874 | Function of proteins | - enzymes (pepsin, DNA polymerase) - structure (keratin, collagen) - carries and transport (hemoglobin, aquaporin) - defence antibodies - movement - muscle | 17 | |
| 8076243346 | Structure of Protein | - monomer = amino acid - polymer = polypeptide chain = protein - 20 different amino acids - protein can be one or more polypeptide chains folded and bonded together | 18 | |
| 8076279882 | Amino acid | - central carbon + amino group + carboxyl group (acid) + R group (side chain) | 19 | |
| 8076311339 | R chain | Variable group gives it chemical distinction | 20 | |
| 8076320755 | Building proteins | - monomers (amino acids) make up the polymer (protein) - peptide bonds: covalent binds between NH2 (amine) of one amino acid and COOH - Polypeptide chains have directions - N-terminus = NH2 end (amino acid) - top - C-terminus = COOH end - bottom - Repeated sequence (N-C-C) is the polypeptide backbone - Function depends on structure --> 3-D structure --> twisted, folded, coiled into unique shape | 21 | |
| 8076369529 | N-terminus | NH2 end (amino acid) - top | 22 | |
| 8076371411 | C-terminus | COOH end - bottom | 23 | |
| 8076375307 | Primary structure | - order of amino acids in chain - Amino acid sequence determined by gene (DNA) - Slight change in amino acid sequence can affect protein´s structure and its function | 24 | |
| 8076393718 | Secondary folding | - local folding - folding along short sections of polyptide - interactions between adjacent amino acid - forms sections of DNA - alpha helix - beta pleated sheets | 25 | |
| 8076419289 | Tertiary structure | - whole molecule folding - interactions between distant amino acids - the structure of a protein that occurs due to interactions between R groups | 26 | |
| 8076454474 | Quaternary structure | - more than one polypeptide chain bounded together - then does polypeptide become functional protein | 27 | |
| 8076580988 | Denaturation | - unfolding of protein - reasons: temperature, pH, salinity - alters 2 and 3 structure - denatured protein is looser and at a more random state | 28 | |
| 8076591994 | Lipids | - composed of C,H,O | 29 | |
| 8076596428 | Family groups of lipids | fats, phospholipids, steroids | 30 | |
| 8076604931 | Fats | - fatty acid - long HC "tail" with carboxyl (COOH) group "head" formed through dehydration synthesis - long HC chain is non polar (hydrophobic) | 31 | |
| 8076637123 | Function of fats | energy storage - concentrated within HC chain - cushion organs - insulation body | 32 | |
| 8076674722 | saturated fats | - all C binded to H - No C=C double bondsC - long straight chains - most animal fat - solid at room temp. - contributes to cardiovascular diseases |  | 33 |
| 8076776175 | unsaturated fats | - C=C double binds in fatty acids - plant and fish fats - vegetable oils - liquid at room temperature |  | 34 |
| 8076803325 | Phosphor lipids | - structure: glycerol and 2 fatty acids and PO4 - PO4 negatively charged - Fatty acid tails = hydrophobic - PO4 head = hydrophilic . split sides | 35 | |
| 8076831089 | amphipathic | hydrophilic and hydrophobic | 36 | |
| 8076944603 | Phospholipids in water | -hydrophilic heads "attracted to H2O - hydrophobic tails "hide" from H2O -can self-assemble into bubbles - semipermeable membrane |  | 37 |
| 8076957697 | Steroids Structure | - 4 fused Carbon rings + something else - different steroids created by attaching different groups to rings - different structure created different function | 38 | |
| 8076978378 | Cholesterol | - important cell component - animal cell membranes - high concentration to cardiovascular disease - more cholesterol the more fluid the cell membrane --> nothing can go through membrane - regulating molecules entering and exiting the cell | 39 | |
| 8077042957 | cell membrane permitted and not | - small lipids can move through - sugar (polar) therefore cannot go through - water, salt is blocked - polar waste is blocked - bilayer is impermeable to polar substances | 40 | |
| 8077105260 | cell membrane channels | - Membranes becomes semi-preambles via protein channels - each channel is very specific - Proteins determine membrane´s specific functions | 41 | |
| 8077135376 | Functions of Membrane of Proteins | - transporters, enzyme activity, cell surface receptors, cell surface identity maker, cell adhesion, attachment to the cytoskeleton | 42 | |
| 8077168373 | Classes of membrane proteins | Peripheral proteins, Integral proteins | 43 | |
| 8077174972 | Peripheral proteins | - loosely bound to surface membrane - Cell surface identity marker - help with transport or communication | 44 | |
| 8077178462 | Integral proteins | - pentrate lipid bilayer usually across whole membrane - transmembrane proteins - transport proteins; channels, permeases (pumps) | 45 | |
| 8077241953 | Diffusion | - 2nd Law of Thermodynamics - concentration gradient | 46 | |
| 8077282985 | Simple diffusion | - move from high to low concentration - diffusion of non polar, hydrophobic molecules - passive transport - no energy needed | 47 | |
| 8077302867 | Facilitated Diffusion | - diffusion through protein channels - channels move specific molecules across membrane - no energy needed - diffusion of polar, hydrophilic molecules | 48 | |
| 8076029479 | 4 major macromolecule classes | carbohydrates, lipids, proteins, nucleic acids | 49 | |
| 8076029480 | Active Transport | - cells may need to move molecules against concentration gradient - protein pump - allosteric change in protein (different shape when engulfing) - requires ATP - against concentration gradient | 50 | |
| 8076024524 | allosteric change | different shape when engulfing | 51 | |
| 8076024525 | Antiport | two molecules are transported to opposite sides | 52 | |
| 8076019787 | Symport | two molecules are transported to the same side | 53 | |
| 8076019788 | Endocytosis (3) | - Phagocytosis: fuse with lysosome for digestion - Pinocytosis: non-specific process - Receptor-mediated endocytosis | 54 | |
| 8076014066 | Phagocytosis | fuse with lysosome for digestion a.Engulfing something large b.Cellular eating c.Specific d.Example: macrophages, neutrophils (immune system) | 55 | |
| 8076011076 | Pinocytosis | non-specific process - cellular drinking | 56 | |
| 8082235156 | Receptor-mediated endocytosis | triggered by molecular signal a.Highly specific b.Lock and key process c.Example: LDL (low density lipids), certain molecules which are needed in the nucleus - signal transduction pathway d.Bind to receptors on membrane e.As a certain number of molecules are attached to receptors the pit deepens | 57 | |
| 8082239826 | Exocytosis | vesicle is leaving the membrane - cellular waste | 58 | |
| 8082242906 | Osmosis | - diffusion of water - following 2nd law of thermodynamics | 59 | |
| 8082250631 | Hypotonic solution | less solute) less concentration of molecules and more concentration of water |  | 60 |
| 8082252949 | Hypertonic solution | (more solute) more concentration of molecules and less concentration of water |  | 61 |
| 8082269572 | Isotonic | concentrations are equal |  | 62 |
| 8082280520 | plant cells osmosis | -normal state is turgid (Hypotonic solution) -Flaccid: not as stable (Isotonic solution) -Plasmolysis: membrane will pull away from wall (Hypertonic solution) | 63 | |
| 8082282237 | animals cells osmosis | -Lysed: cell bursts (Hypotonic solution) -Normal: Isotonic solution -Shrivelled: Hypertonic solution | 64 | |
| 8082290028 | Why are cell so small | -The greater the surface area the more surface for diffusion to go across -The larger the surface area to volume ratio the faster the rate of diffusion into a cell | 65 | |
| 8083978974 | Types of microscopy | -Light microscope -Electron microscope -Scanning electron microscope -Transmission electron microscope | 66 | |
| 8083981779 | cell theory | - cell come from other cells - living things are made from cells | 67 | |
| 8083985586 | Characteristics of life (MRS GREN) | - Communication - Reproduction - Order - Growth and development - Energy processing - Regulation - Response to environment - Evolutionary adaption | 68 | |
| 8084008257 | surface:volume ratio | Smaller cells can diffuse more at a faster rate because of their higher surface to volume ratio | 69 | |
| 8084013251 | Prokaryotic cells | - bacteria and Archea | 70 | |
| 8084013252 | Eukaryotic cells | - smaller and simpler - protists, plant, fungi, animal - membrane enclosed nucleus | 71 | |
| 8084024476 | Similarities between Eukaryotic and Prokaryotic cell | -Cytosol -Chromosomes -Ribosomes -cytoplasm | 72 | |
| 8084028103 | Plant vs Animal cell similarities | -membrane bound organelles such as nucleus, mitochondria, endoplasmic reticulum, goldi apparatus, lysosomes -similar membranes, cytosol and cytoskeleton | 73 | |
| 8084032294 | Plant differences | -larger than animal cells -chloroplasts -Vacuoles -Cell wall | 74 | |
| 8084059784 | Mitochondria | carry out cellular respiration | 75 | |
| 8084061432 | Chloroplast | photosynthesizing organelles of plants and algea | 76 | |
| 8084064654 | Nucleus | contains cell´s genetic instructions encoded in DNA - directing protein synthesis | 77 | |
| 8084069590 | Ribosomes | make proteins | 78 | |
| 8084071314 | endoplasmic reticulum | an internal membrane system in which components of cell membrane and some proteins are constructed | 79 | |
| 8084081159 | Endosymbiotic theory | states that mitochondria and chloroplasts were formerly small prokaryotes that began living within lager cells | 80 | |
| 8084233058 | cytoskeleton | jelly like fluid that fills a cell | 81 | |
| 8084236073 | flagella and cilia | protude cell membrane and make wave like motions | 82 | |
| 8084242157 | flagella | long and few | 83 | |
| 8084243958 | cilia | short and many | 84 | |
| 8084260964 | Extracellular matrix | - hold cell together - made of glycoproteins | 85 | |
| 8084263693 | Glycoproteins | carbon with protein | 86 | |
| 8084267106 | cell junction | -consist of multiprotein complexes -provide contact between neighbouring cells or between a cell and the extracellular matrix | 87 | |
| 8084327876 | Fluid-mosaic model of cell membranes | flexible layer made of lipid molecules is interspersed with large protein molecules that act as channels through which other molecules enter and leave the cell | 88 | |
| 8084342224 | Types of protein in membrane | -Transporter -Enzyme activity -Cell surface receptor -Cell surface identity marker -Cell adhesion -Attachment to the cytoskeleton | 89 | |
| 8084345651 | Transporter protein | allows substances to cross the membrane through a channel in its interior | 90 | |
| 8084347448 | Amphipathic | hydrophilic ("water-loving") or polar end and a hydrophobic ("water-fearing") or nonpolar end | 91 | |
| 8084375005 | What can go through the membrane? | small nonpolar molecules | 92 | |
| 8084439436 | Spontaneous membrane formation | - phospholipids can self assemble into simple molecules - a membrane can enclose a solution that differs from its surrounding - basic requirement of life: plasma membrane that allows cells to regulate their chemical exchanges with the environment | 93 | |
| 8084456265 | Aquaporin | form pores in the membranes of cells and selectively conduct water molecules through the membrane, while preventing the passage of ions | 94 | |
| 8084457999 | Ion channel | -ability to open and close in response to chemical or mechanical signals -open: ions move through channel in single line fashion -ion channels are specific to particular ions | 95 | |
| 8084460551 | Water potential | potential energy in water - how willing is it to move | 96 | |
| 8084463880 | Water potential equation | Water potential = Solution potential + pressure potential | 97 | |
| 8084468292 | Solution Potential | -iCRT | 98 | |
| 8084470758 | Gibbs Free Energy eq | ΔG = ΔH - TΔS | 99 | |
| 8084472346 | Gibbs Free Energy | The energy of a system available to do work | 100 |
