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65 Cards in this Set
- Front
- Back
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Hierarchy
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Biosphere
Ecosystem Communties Population Organisms Organ Systems Organs Tissues Cells Organelles Molecules |
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Plasma Membrane Structure
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Phospholipid bilayer embedded with proteins and carbohydrates
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Passive Transport
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No ATP
Direct Passage: Small hydrocarbons, steriods, and small non polar molecules pass through phosophlipid bilayer Facilitated Diffusion: diffusion of those molecules through proteins without ATP proteins like channel protiens and carrier proteins |
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Active Transport
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uses ATP to transport molecules through protein
Ex: Proton Pump uses ATP to bring H+ out of cells Sodium Potassium Pump: 3 sodiums go out of cell 2 potassiums go in cell and it uses ATP |
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Vesicular Transport
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2 Types:
Endocytosis: brings stuff inside cell 3 Kinds: Phagocytosis:cellular eating eats specific stuff Pinocytosis:cellular drinking eats everything Receptor mediated endocytosis: receptors identify certain molecules and pinches in Exocytosis: puts stuff outside |
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Cytoskeleton
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Found throughout cytoplasm
-allows for support and movement |
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What are the 3 kinds of cytoplasm?
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microtubules, microfilaments, and intermediate filaments
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Microtubules
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in cytoplasm added and subtracted from positve end
-Hollow cylindrical rods made of tublin dimers -make up flagella and cillia Function: cell shape -function as a track for movement of components within cell over long distances Ex: vesicles and organelle movement and chromosome movement during cell division requires interactions with motor proteins -Kinesin(+) goes to plasma membrane -Dyenin(-) goes to nucleus |
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Microfilaments
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in cytoplasmic mesh
Structure: double chain of actin subunits Assembly/Disassembly: subunits added and subtracted from oppostite ends Function: cell shape, movement of short distances Cell Motility: contraction of actin and myosin(motor protein) -extends the pseudopodia |
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Mitochondria
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-have membranes, but not part of endomembrane system
-energy transformers -semiautonomous: grow and reproduce within cell location is not fixed. it moves on cytoskeletal tracks. more than 1 mitochondria per cell. has a outer membrane, inner membrane, inner membrane space,cristae, free ribosomes, matrix, mitochondria DNA |
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Chloroplast
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in leaves and plants
their shape is plastic and tey can reproduce themselves by pinching in two ribosome, stroma, inner and outer membrane, granum, thylakoid, DNA |
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Nucleus
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genetic library of eukaryotic cells
chromatin: DNA and associated proteins mRNA synthesis has double membranes and pores |
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Nucleoulus
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rRNA synthesis-found in ribosomes
Makes up ribosomal units |
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Ribosomes
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synthesize protein
-made up of proteins and rRNA -2 subunits one large one small -no membrane 2 types of ribosomes: Free Ribosomes-synthesize cytosolic proteins Bound Ribosomes-synthesize integral membrane(transport) and secreted proteins |
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Endoplasmic Reticulum
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-continuous with nuclear envelope
-cisternae: internal space |
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Smooth ER
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rich in metabolic enzyme
-ribosome free special cells have a lot of ER -makes lipids -breaks down carbohydrates -detoxification of drugs and poison -holds calcium |
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Rough ER
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-prep proteins for delivery that are formed on bound ribosomes
-secreted proteins and membrane proteins made by ribosomes and processed by ER |
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Golgi Apparatus
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finishes, sorts, and ships
-flattened membraneous sacs cis face: recieving side trans face: shipping side -ER vesicles fuse with cis face -each cisterna contains specific enzymes -makes polysaccarides -transport out of Golgi |
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Lysosome Formation
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made in rough ER
-enzyme and membrane created in Rough ER -lysosome membrane isolates disgestive enzyme from rest of cell |
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Proton Pump
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makes inside have low pH of 5
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Lysosome enzymes
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works best in low pH
hydrolyze proteins, fats, polysaccharides and nucleic acids |
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What do lysosomes fuse with?
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vacuoles to digest food
-recycle damaged organelles -phagosomes to destroy invaders |
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Tay-Sachs
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lysosome deficent disease
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4 classes of signal molecules
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1) secreted signals that act locally
2) secreted signals for long distance 3)intracellular signals 4) cell surface signals |
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Secreted Signals that act locally
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a) paracrine signaling- growth factors
b) synaptic signaling- neurotransmitters |
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Secreted cells for long distance
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travels through circulatory system in animals.
for plants: vessels, cell to cell, or diffusion in air |
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Intracellular Signals
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a) cell junctions
ex. gap junctions between animal cells plasmodesmata between plant cells |
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Cell surface Signals
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a) cell to cell recogniition
ie. blood antigens and antibodies |
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Cell signaling process
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reception
transduction response |
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Reception for Cell Signaling
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ligands change location/shape of receptor protein
-plasma membrane proteins- ligands are secreated and water soluable in paracrine and synaptic and membrane bound in cell surface signals -cytoplasmic or nuclear proteins- ligands need to be lipid soluable in order to pass through membranes |
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Specific types of plasma membrane receptors
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G Protein linked receptors: ligands are hormones and neurotransmitters
Tyrosine Kinase Receptors: ligands are growht factors Ligand gated ion channels: ligands are neurotransmitters Cell to Cell communication: receptor proteins on white blood cells bind to antibodies that are bound to surface of bacteria. this stimulates phagocytosis |
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Intracellular Receptors
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-receptor proteins are inside cell rather than on the surface
-ligands are steroids that can go through membrane -receptor proteins can be found either in cytosol or nucleus |
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Living matter is made up of?
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96% is made from C, O, N, H
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Out of 92 elements, how many are essential to life?
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25
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Types of Bonds
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covalent- non polar and polar
ionic- ex: Na+Cl- hydrogen: only occurs in polar molecules. weak attraction force between dipoles. |
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Functional Properties of Water
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1.Cohesion- water molecules are attracted to each other
-each water molecule can be attracted to 4 others at a time 2.Solvent- dilute solute to decrease concentration or hold solute -it dissolves polar molecules and repels non polar molecules |
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Acids
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increase H+ in solutions
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Bases
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decreases H+ in solutions
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Buffers
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resist change in pH of solution
-donate H+ when in excess -Accept H+ when depleted |
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What's the pH of Human Blood? And what is it buffered by?
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pH 7.4
carbonic acid and bicarbonate H2CO3--> HCO3- + H+ acid base hydrogen ion |
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Carbon bonds to what?
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C,H,N,O,P,S
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carbon based compounds make what?
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carbohydrates
Lipids Proteins DNA |
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Factors contributing to molecular diversity
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1. large variation of carbon skeleton
2. functional groups that replace H (like hydroxyl, carbonyl, carboxyl, sulfurhydral, amino, and Phosphate) |
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Carbon based macromolecules
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carbohydrates, proteins, nucleic acids are made up of polymers
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Polymers
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long molecules built from small similar subunits(monomers) linked by covalent bonds
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What are lipids made out of
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two or more different subunits.
hydrophobic which means it has a nonpolar covalent bond. |
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What are the two ways to Form or dissasemble polymers?
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Dehydration- loss of water and then it joins
Hydrolysis-addition of water and ten they break apart |
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Carbohydrates
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sugars and their polymers
1) monosaccharides- 3,5,or 6 carbon sugars monomer a building block of carbs 2)disaccharides- 2 monosaccarides joined by glycosidic linkage -uses dehydration to put them together 3) polysaccharides- 100-1000 monosaccharides -found in cellulose and cell wall of plants, maitins structure |
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In what form energy stored in plants and animals?
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plants- startch
animals- form of glycogen |
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What are the forms of Lipids?
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Fats, Phospholipids, and Steriods
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Fats
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composed of glycerol(head) and 3 fatty acids (tails)
uses dehydration to form 2 kinds of fats: -saturated:packed closely, no double carbon bonds ex: butter -unsaturated: has double carbon bond, has kinks which doesnt allow it to package closely ex: oil |
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Phospholipids
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made up of
Glycerol+2 fatty acids+phosphate+choline phospholipid bilayer |
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Steroids
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carbon skeleton with four rings and varying functional groups
-ex: cholestrol -found in membrane -precursor to testostrome and estrogen |
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Protein Functions
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-enzyme(catalyzes stuff)
-support -transport -signaling/ transport |
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Structure of Protein
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amino acids-> monomers-> polymers(polypeptides)-> protein
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Levels of Proteins
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primary-sequence of amino acids determine protein
secondary- alpha or beta helix hydrogen bonded tertiary- R group interactions -weak: hydrogen bond, ionic bond, and vander waals attraction quanternary- 2 or more polypeptide(oligomer) |
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What in the environment is the protein influenced by?
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pH, salt, and temperature
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What happens to damaged proteins?
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-tagged by ubiquitins
-delivered to proteosomes -proteases chops protein into short peptides for reuse or chapperone protein comes and folds it |
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Nucleic Acids Functions
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store and trasnmit hereditary information
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Purines
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two rings
Adenine or Guamine for DNA For RNA it's Uracil |
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Pyridmidines
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One ring
cyotsine or thymine |
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How does DNA copy?
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1.mRNA synthesis
2.moves out of nucleus 3. protein synthesis with ribosomal subunits |
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Structure for ATP
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3 phosphate+ Ribose+ adenine
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exergonic
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when energy goes from high to low
-change in G is less than 0 |
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endergonic
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when energy goes from low to high
-change in G is greater than 0 |
