Vesicle
2 GTP
Pyrimidine
Purine
Hydrogen Bonding
Transport Vesicle
Transport Vesicle
Cellular Respiration Relation to Metabolic Pathways
tRNA moves to
Anit-Codon and Codon pairing
Transport Vesicle
tRNA moves to
Complementary Base Pairing

Concept Map 1

Water

States of Water

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Solid state = hydrogen bonds form and DO NOT break Strong, ordered crystal lattice structure Expansive upon freezing Liquid state = hydrogen bonds break and reform constantly (Denser state than solidGas state = hydrogen bonds break and DO NOT reform

Universal Solvent

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Dissolve = water seeps inside crystal lattice and surrounds each ion (hydration shell) to break bonds Ionic compounds dissolve in water through Ion-Dipole interactions (ie salt) Polar compounds dissolve inw ater through Hydrogen bonds (ie sugar)Water SURROUNDS Nonpolar compounds because they are Hydrophobic

Cohesion

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Allows for water movement against gravity in plants due to hydrogen bonds between water moleculesCauses high surface tension in water - makes it difficult to break water surface

High Specific Heat

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Helps moderate temperature - defined by amount of heat required to raise temperature by 1 degreesWater absorbs heat --> hydrogen bonds break --> water releases heat and bonds reform = water is resistant to changes in temperature

High Heat of Vaporization

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Amount of heat/kinetic energy absorbed is high enough to break hydrogen bonds and NOT reform Evaporation Cooling = stabilizes temperature in water and organism by cooling surface after water evaporates

Proteins

Protein Folding

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Primary Structure: Long chain of amino acids Involves MAIN chain of aminosPEPTIDE Bonds are present Secondary Structure: Alpha helicase or Beta pleated sheetsInvolved MAIN chain of aminos HYDROGEN Bonds are present Tertiary Structure: Polypeptide fold into 3D shape Involves R GROUP ALL Bonds are present Disulfide, Ionic, Hydrogen, Hydrophobic, and Van der Waals Quaternary Structure: 2+ Polypeptides form functional protein Involves R GROUPALL bonds are present

Denuturation

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Environment alters/heats = Protein cannot retain shape = UNFOLDS back to PRIMARY STRUCTURE Breaks all bonds EXCEPT PEPTIDE BONDSRenature (remove denaturing condition) is successful IF the protein retains original function -- ie cool protein if heat caused denature

Amino Acid Monomer

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Central Carbon bonded to 4 DIFFERENT groups = Enantiomer Isomer (mirror images) ONLY L FORM OF ENANTIOMER PRESENT Link together through dehydration to form Polypeptides Protein functions as Trimer = 3 Polypeptides --> Highest structure = Quaternary Protein function as Dimer = 2 Polypeptides --> Possible structures = Primary, Secondary, Tertiary, Quaternary

R Groups

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Side Chain = R Groups Non Polar (C-H): Hydrophobic and Van der Waals interactions N-H can be both non polar or polar but is GENERALLY MORE NON POLAR Polar (O-H, S-H, C=O): Polar Covalent interactions Acidic: Negatively charged Basic: Positively charged Glycine is NOT an Enantiomer because there are not 4 unique groups around central Carbon

Main Chain

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Main Chain = Amino (NH2+), Carboxyl (COOH-), and Hydrogen SAME FOR ALL AMINO ACIDS

Functions

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Enzymatic Proteins = Accelerates selective chemical reactions Defensive Proteins (ANTIBODIES) = Protection against disease Storage Proteins = Stores amino acid monomers Transport Proteins = Transports substances through cell Hormonal Proteins = Coordinates an organism's activities through secretion of hormones (ie Insulin)Receptor Proteins = Helps with cell response to chemical stimuli Contractile + Motor Proteins = Cell movement (ie Myosin and Actin in muscles) Structural Proteins = Cell support (ie Collagen and Keratin)

Joey

Carbohydrates

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Carbohydrates are organic molecules that serve as energy fuel for short-term storage. Carbohydrates are one of the biomolecules that contain monomers and polymers. The monomers of carbohydrates are called monosaccharides while the polymers of carbohydrates are polysaccharides.Carbohydrate skeletons can be drawn in four structures: linear, double bond position, branching, and rings.

Polysaccharides

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Polymers are synthesized through dehydration/condensation. Polymers are broken down via hydrolysis and enzyme catalysts.There are different types of polysaccharides: storage and structure.

Storage Polysaccharides

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Storage polysaccharides

Glucose

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The difference between all the types of polysaccharides is the type of linkages they have and whether or not they are alpha glucose or beta glucose.

Glycogen

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What we would think of when we think glucose. Glycogen is a large, formed polysaccharide that is used by the body as fuel. It uses alpha 1-6 glycosidic linkage to branch out the glucose to store energy to use for fuel.

Cellulose

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Cellulose is a beta glucose molecule and to make the structure of cellulose found in the cell membrane, it uses beta 1-4 glycosidic linkage. Enzymes cannot be used to break down the linkages, so it is not digestible. Another type of structure polysaccharide is chitin, which is also found in plant cells.

Amylose

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Amylose uses alpha 1-4 glycosidic linkage to form helix chains. Amylose is not soluble in water and doesn't produce a gel when hot water is present.

Amylopectin

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Amylopectin uses alpha 1-6 glycosidic linkage to form branched helix chains. Amylopectin is soluble in water and does produce a gel when hot water is present.

Structure Polysaccharides

Monosaccharides

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Monosaccharides are monomers that are simple structures like glucose, fructose, and galactose.

Bonds

Intermolecular

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BETWEEN MOLECULES

Hydrogen

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Hydrogen bonding with F, O, N of adjacent molecule POLAR INTERACTION

Van der Waals

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Asymmetric electron distribution in molecules Electrons pull towards partial positive side NON POLAR INTERACTIONHappens everywhere

Hydrophobic

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Non Polar parts group together in Polar substance (Water) NON POLAR INTERACTION Seen in Phospholipid tails

Ion Dipole

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Between ions and polar molecules 1 fully charged and 1 partially charged (ie Na+ and Cl- interacting with H2O partial charges) Positive charge interact with negative charge 

Intramolecular

Ionic

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Ionic - electrons transferred from one atom to another producing a cation and anion

Colavent

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Covalent - electrons shared between two atoms under the same electron cloud (ΔEN >1.5)

Nonpolar

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Nonpolar covalent - electrons equally shared between two atoms (ΔEN <0.5)

Polar

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Polar covalent - electrons unequally shared between two atoms (ΔEN 0.5<x<1.5)

Nucleic Acids

DNA

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Deoxygenated pentose sugar with a phosphate group and nitrogenous bases (A, T, C, G) Double helix structure easy for stability and replicationHydrogen bonds with nitrogenous bases and phosphodiester linkages

RNA

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Oxygenated pentose sugar with a phosphate group and nitrogenous bases (A, U, C, G)Alpha bent structure making it easy for replication and systemization of proteinsNo hydrogen bonds with nitrogenous bases and phosphodiester linkages

Andrew

Eukaryotic - The Basics

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To not go too much into structure, this is just the basics of Eukaryotic cells. Eukaryotic cells are very complex cells that have different organelles across different cell types.Common Organelles:Nucleus - A complex envelope that contains Deoxyribose Nucleic Acid that contains the instructions for the cell for its function and the template to create amino acids. Mitochondria: Often called the "Powerhouse" of the cell, this is where the synthesis of ATP is done. Rough and Smooth Endoplasmic Reticulum - A network of membranes involved in protein synthesis and folding. Rough ER has ribosomes embedded within it. Smooth ER is involved in Lipid synthesis. Golgi Apparatus - Modifies, sorts, and packages proteins and lipids for transport. Lysosomes: Contain enzymes that break down waste products and cellular debris through the acidic interior of Lysosomes. Ribosomes: Small structures that are responsible for protein synthesis through tRNA and rRNA.Plasma Membrane: The outer boundary of the cell, and it regulates what enters and exits the cell. Chloroplasts: Organelles that capture sunlight for photosynthesis for glucose. These are pretty common organelles but multiple Eukaryotes have cell-exclusive organelles:Flagella for movement through fluidPili for attachmentAxons, Mylean Sheeth, etc. for nerve cells.

Differences Between Eukaryotic & Prokaryotic Cells & Endosymbiotic Theory

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Prokaryotic - Basic small cells with a limited number of organellesEukaryotic - Complex larger cells with the presence of membrane-bound organelles Endosymbiotic TheoryProkaryotes were the first cells with Eukaryotes coming after. The proposed theory states that a protoeukaryotic cell absorbs a prokaryotic cell to make Mitochondria, and an autotrophic prokaryotic cell makes Chloroplasts. Evidence for the Endosymbiotic Theory The inner membranes of mitochondria and plastid are similar to the plasma membranes of living bacteriaReplication of mitochondria and plastids is similar to cell division in BacteriaMitochondria and plastids have circular DNA like Bacteria Mitochondria and plastids transcribe their own DNA into proteins. There are Ribosomes in mitochondria - almost having an independent cell structure

Lipids

Structure

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Lipids are made from building blocks of sugar:One - Monosaccharides Two - DisaccharidesThree - TrisaccharidesFour or More - Polysaccharides These saccharides link through the Glycolic Cvalend bond - meaning water performs a hydrolysis reaction that breaks this bond. Fructose and Glucose come in contact and allow water to use hydrogen bonds.Types of Polysaccharides Storage PolysaccharidesGlycogen Starch Dextran Structure Polysaccharide Cellulose Chitin Glycerol fatty acids can have multiple chains formed through ester bonds. Tails that contain only a single bonded chain are called saturated fats. Tails that contain double bonds are called unsaturated fatsTrans geometric structures cases have the hydrogens on both sides of the double bondCis geometric structures cases have the hydrogen on the same side of the double bond; this results in a large bend on the hydrocarbon tail.

Function

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Lipids are one of the most important molecules for cells to have function:Cellular Membrane: Lipids are fundamental components of cell membranes. Usually phospholipids, these form a structure having hydrophilic facing the outside of the cell and the inside surface of the cell, with the hydrophobic hydrocarbon tails between the membrane. Energy Storage: Lipids serve as a dense source of energy for cells. In animals, fats like triglycerides are stored in cells to provide energy when glucose levels are low Some other functions that are not covered are insulation/protection for macroscopic organisms, Signaling Molecules, and Electron carriers in cellular respiration.

Prokaryotic - The Basics

Bacteria - Basics

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Bacteria are small simple cells that consist of a fundamental Cell Structure.These usually consist of CytoplasmMembraneChromosomes folded within a Nucleoid A small collection of DNA in certain Bacterial cells have a Plasmid. Plasmids can also be exchanged between Bacterial cells. This is how antibiotic-resistant genes are transferred between Bacterial Cells.Cell WallsUniquely Cell walls are made from Peptidoglycan instead of Cellulose & Beta-Glucose in plant cells. Certain Bacteria also contain:Slime layers that are made of PolysaccharidesSome Bacteria have Flagellum to propel through solvents like water. Motile function.Some have fimbriae and pili that attach to surfaces. hey can also use pili to connect to bacteria and transfer DNA - Plasmid Anti-biotic Resistance Some can form endospores which is a hibernation almost where Bacteria can survive in harsh conditions for centuries. Other minor organells:Gas VacuolesRibosomesInclusion BodiesNucleoidsPeriplasmic Space

Differences Between Kingdoms

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While the Kingdoms might be similar, there are a few major differences, like their organelles:Both have the presence of cell walls.Both do not have a nucleus Archaea has branched lipids that are uniquely made with ether bonds. Bacteria do not.Bacteria have the presence of peptidoglycan, whereas Archaea does not.

Bacterial Metabolism

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There are four major nutritional modes of Prokaryotes Autotrophic MethodPhotoautotrophs ChemoautotrophsHeterotrophicPhotoheterotrophicChemoheterotrophicRoles of Oxygen in Metabolism Obligate aerobesRequires Oxygen for Cellular Respiration Obligate anaerobesUses fermentation and anaerobic respiration. Poisoned by Oxygen.Facultative anaerobesUses Oxygen when present. Carry out fermentation or anaerobic respiration when Oxygen is not present.

Archaea - Basics

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Archea is rumored to be one of the first-ever cells of life. They are extremely basic, yet this simple structure provides the basis for a stable organism and some unique properties.Some Archea live in extreme environments, these are called extremophiles Extreme Halophiles - Can survive in high-solute solutions Extreme Thermophilies - Can survive in extreme temperaturesAcidophiles - Can survive in acidic solutions

Archaea Metabolism

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Some Archaea are Methanogens, which live in swaps and marshes. These produce Methane a waste product of their metabolism. This provides those environments with a "rotten" smell.

Plant Cells Only

Concept Map 2

Cellular Respiration

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CATABOLIC REACTION (exerting energy) Electron Carriers: NADH and FADH2Glucose = Oxidized, Oxygen = Reduced

Glycolysis

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Starts with electrons from food (glucose) Occurs with or without oxygen (anaerobic and aerobic) Energy Investment Phase Uses 2 ATPCreates 2 G3PEnergy Payoff Phase Makes 4 ATP Everything is doubled

Step 1

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Start: Glucose Add: Hexokinase Removes Phosphate group from ATPEnd: Glucose 6P + ADP

Step 3

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Start: Fructose 6PAdd: Phosphofructokinase End: Fructose 1-6 Bisphosphate

Output

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"I take a NAP @ 2PM"NET: 1 Glucose = 2 NADH, 2 ATP, 2 Pyruvate

Pyruvate Oxidation

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Needs Oxygen (Aerobic) Pyruvate from Glycolysis gets oxidized in the Mitochondria if O2 is present Products go through Krebs/Citric Acid Cycle

Output

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1 Pyruvate = 1 Acetyl CoA + 1 NADH

Oxidative Phosphorylation

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Occurs in Mitochondria Goal is to generate ATP

Electron Transport Chain

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Electrons from NADH travel through Complexes I, Q, III, C, and IV down ELECTRON TRANSPORT CHAIN Complexes I, III, and IV pump out H+ into the intermembrane spaceEnergy from electrons transferring down ETC is used to pump H+ AGAINST concentration gradient Once electrons reach Oxygen, water is formed

Chemiosmosis

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H+ traveling AGAINST gradient from ETC supplies energy source to convert ADP to ATP as it travels DOWN to Chemiosmosis ATP Synthase is involved Synthase grabs protons pumped out as electrons travel down ETC - Facilitated Diffusion

Citric Acid Cycle

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Occurs in the Mitochondria

Step 1

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Start: Oxaloacetate Add: Acetyl CoAEnd: Citrate

Step 3

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Start: Isocitrate End: Alpha Ketoglutarate

Output

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1 Acetyl CoA + 1 NADH = 1 ATP, 3 NADH, 1 FADH2

Fermentation

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Occurs in cytoplasm, without Oxygen (Anaerobic) RECYCLING PROCESSRecycles NADH into NAD+ to generate more Glycolysis

Alcohol

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Start: 2 NADH + 2 Pyruvate End: Lactate

Lactic Acid

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Start: 2 NADH + 2 Pyruvate End: Ethanol + Carbon Dioxide

Cell Signaling

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Notes

Local Signaling

Synaptic Signaling

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Electrical signals along nerve cells trigger a release of neurotransmitters that diffuse across the synapse to reach the target cells so that they can become stimulated and get the signal.

Paracrine Signaling

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Local regulators (or signals or ligands) diffuse through the extracellular fluid to get to the target cell.

Membrane Receptors

G-Protein-Linked Receptor

Phosphorylation Cascade

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Here, we'll look at an example of the amplification effect caused by binding epinephrine to the receptor and causing millions of molecules to be made.

Epinephrine binds to G-Protein-Linked Receptor

Inactive G-Protein is activated and slides across the membrane to bind and activate Adenylyl Cyclase

ATP is used to activate Adenylyl Cyclase

Activated Adenylyl Cyclase converts ATP to Cyclic AMP (cAMP) as a secondary messenger

cAMP activates a series of Protein Kinases

Cellular Response (millions of molecules)

Phosphodiesterase (PDE) deactivates cyclic AMP (cAMP) and converts it to AMP

Protein Phosphatase (PP) removes a phosphate group to deactivate the proteins

After the G-Protein activates Adenylyl Cyclase, it can continue to activate the enzyme or deactivate by delinking a phosphate group from GTP and making GDP and shift back to it's origin

The ligand can stay on the receptor and continue the amplification effect or dissociate from the receptor and end the effect

Ion Channel Receptor

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Ion channel receptors often have ligand-gated receptors in which the channel will remain closed until a ligand binds to the receptor. When the ligand binds to the receptor and the channel opens, specific ions can flow through the channel and rapidly change the concentration of that particular ion inside the cell. This change may directly affect the activity of the cell in some way. When the ligand dissociates from this receptor, the channel closes and ions no longer enter the cell.

Ligand binds to receptor

Channel opens allowing ions to flow down the concentration gradient

Ions enter the cytoplasm and trigger a cellular response

Ligand dissociates and channel closes

Intracellular Receptors

Signaling Molecule

Long-Distance Signaling

Hormonal Signaling

Steroid Hormone Receptors

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The steroid hormone, aldosterone, passes through the plasma membrane. Aldosterone binds to an intracellular receptor protein in the cytoplasm, activating it. The hormone-receptor complex enters the nucleus and binds to specific genes. The bound protein acts as a transcription factor, stimulating the transcription of the gene into mRNA. The mRNA is translated into a specific protein.

Epinephrine

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One steroid hormone can have multiple effects on cells. If can have the same receptor but different intracellular proteins to activate, or it can have different receptors.

Eukaryotic Cells

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DEFINED BY:DNA in nucleusDouble membrane bound organelles EXTERNAL MEMBRANE:Glycolysis FermentationINTERNAL MEMBRANE: Pyruvate Oxidation Citric Acid/Krebs Cycle

Plants ONLY

Chloroplast

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Site of plant photosynthesis Contains: Stroma = Internal fluid Thylakoid = Membrane sacs Stacks of Thylakoid = Granum

Plasmodesmata

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Cell junction in plants Provides channels for water and nutrients to travel between cells

Cell Wall

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Made of celluloseMaintains cell shape Contains: Secondary Cell Wall: Between plasma membrane and primary cell wallPrimary Cell Wall: Thin + flexible Middle Lamella: Between primary walls of adjacent cells

Both Plants and Animals

Endomembrane System

r

Responsible for protein traffic + metabolic functions

Endoplasmic Reticulum

r

Contains:Smooth ER (NO Ribosomes) = Makes Lipids, metabolizes Carbs, detoxify DISEASE = JAUNDICERough ER (Bound Ribosomes) = Folds Proteins, secretes Glycoproteins

Golgi Apparatus

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Shipping Vesicle Contains: Cis Face = Receiving sideTrans Face = Shipping side

Vacuoles

Food Vacuole

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Formed when Phagocytosis occurs

Central Vacuole

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IN PLANTS ONLY Stores Potassium, Water, and Chloride

Contractile Vacuole

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Pumps excess water out of Freshwater Protists

Lysosome

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H+ pump maintains LOW PH INSIDE to keep enzyme functional = Hydrolysis/breaks covalent bondsDISEASE = Build up of toxins

Phagocytosis

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EATCell extends membrane --> Engulf ---> Pinch offDigestion products (amino acids + simple sugars) --> Cytosol as nutrients

Autophagy

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RECYCLEHydrolysis enzyme recycles organic materials Digests damaged organelles --> Cytosol for reusage

Nuclear Envelope

r

Regulates transport in + out of nuclear pores

Ribosomes

Bound Ribosomes

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Present OUTSIDE ER Protein inserted in membrane/secreted out of cell

Free Ribosomes

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Present in CYTOSOL Makes Proteins

Mitochondria

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Site of cellular respiration Contains:Intermembrane SpaceCristae: Membrane foldsMitochondrion Matrix = Free ribosomes + DNA Involved in Cell Respiration to make ATP = POWERHOUSE OF CELL DISEASE = Myoclonic Epilepsy

Cytoskeleton

r

Cell Storage + Organelle Anchorage

Microtubules

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ALL EUKARYOTES HAVE THICKEST (Alpha and Beta Dimers) Contains:Dynein = Motor protein to drive bending movement of organellesBasal Body = Ring of 9 triplets to anchor Cilia + Flagellum DIFFER in arrangement of microtubules

Microfilaments

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THINNEST = made of 2 intertwined actin protein strands Actin Filaments

Muscle Contraction

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Myosin head + Actin filament attach and move = actin filament slides = underlying muscle fibers contract

Amoeboid Movement

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LOCALIZEDMicrofilament + Myosin = Tail squeeze interior fluid = Extending Pseudopodium

Cytoplasmic Streaming

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LOCALIZEDMyosin contract in PLANTS = Propels Cytoplasm = Distribution of nutrients

Intermediate Filaments

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MORE PERMANENTMaintains cell shape, anchors nucleus + organelles, forms nuclear lamina Made of KERATIN Proteins

Nucleus

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Site of Transcription + DNADISEASE = Progeria

Nuclear Lamina (TEM)

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Gives shape to nucleus

Nucleolus

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Site of rRNA synthesis

Nuclear Pores

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Helps transport in and out of nucleus

Specialized Cells

Lymphocytes

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B Cells = MAKE ANTIBODIES to bind to + destroy antigens Increased Ribosomes and Golgi Apparatus (ship out through ER)

Macrophage

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Break down + release toxin (engulf + destroy) Increased Lysosomes

T Lymphocytes

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T helper cells activate B cells B + T interact through surface proteins Increased Ribosome, Rough ER, Golgi (for transport)

Animals ONLY

ECM

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ECM changes = changes in cell MNEMONIC: "Can Find Party In ECM rave"

Proteoglycan

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Made of protein + sugarAttached to single polysaccharide

Integrins

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Binds to ECM = Transmit signals between inside and outside of cell

Collagen Fibers

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Embedded in web of Proteoglycan complexes

Fibronectin

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Attach ECM to Integrins in Plasma Membrane

Junctions

Tight Junctions

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Nothing goes through

Desmosomes

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Leaky junctions Point of direct contact between cells

Gap Junctions

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Everything goes through

Metabolism/Enzymes

The Metabolic Pathway
Maintain Homeostasis

Types Include:
Cellular Respiration via
Glucose is oxidized.

Additional:
Anabolic Pathways such as
Polymerization and Photosynthesis

Conservation of Energy

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Thermodynamics System - matter within a defined region of space Closed SystemOpen System Laws of Thermodynamics First Law of Thermodynamics: Energy can be transferred and transformed, but cannot be created or destroyed. Second Law of Thermodynamics: Every energy transfer or transformation increases the entropy of the universe.

Free Energy & Free Energy Change

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Free Energy is Cellular WorkEntropy = Gibs Free Energy + T(Enthalpy)G = H -TSMeasuring change in each at constant of TFree-Energy Change (ΔG)The change in free energy ΔG during a chemical reaction is different between the free energy of the final state and the free energy of the initial state ΔG = G(final) - G(inital)For a spontaneous process, no energy input is needed - ΔG is negativeFor a nonspontaneous process, energy input is needed ΔG is positive

Ideally in life, we want most reactions to be ΔG<0

Enzymes

Overall Goal:
Speed up Chemical Reactions

Lower Activation Energy
of Reactions to Take Place

Made of Specialized Proteins
with An Active Site

Enzymes are also pH and Temperature Sensitive.

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Most Enzymes have an ideal pH or Temperature that they work at most efficiently, and when these fall outside the parameters the enzyme not might work as well or overall completely denature back to a polypeptide chain.

Competitive Inhibior

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Competitive Inhibitors bind to the active site of a enzyme prevent substrates from binding to the enzyme and lower overall efficiency of reactions.

Noncompetitive Inhibitor

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Binds to another part of the enzyme but affects the shape so that original substrates cannot bind to the new active site

Membrane - Basics

Plasma Membrane - Outer
Layer of the Cell

Membrane Proteins

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Membranes have a variety of proteins Peripheral proteins are not fully integrated within the cellsIntegral proteins are integrated fully within the membrane Some Functions of Membranes Proteins Include:TransportEnzymaticSignal TransductionCell-Cell Recognition

Membrane Fluidity

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Membrane Fluidity Each phospholipid has a specific phase transition temperatureAbove this temperature, lipids are in a liquid crystalline phase and are fluid Below this temperature, lipids are in a gel phase and is more rigid

Membrane Permeability

Selective
Permeability

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Selective permeability of Plasma Membrane General rule is the size and charge of the molecule can in and out of the cellTransport proteins allow the passage of hydrophilic substances across the membrane

Active Transport

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Movement of substances from low to high concentrations (pushing against the concentration gradient)Maintains a concentration gradient Uses energy (ATP)

Carrier
Protein
Pump

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Carrier Protein Pump: Carries from protein from inside to outside the cell, uses ATP energy to change shapes within the molecule

Electrogenic
Pump

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A transport protein generates a voltage across a membrane-membrane potential Help stores energy that can be used for cellular work

Proton Pump

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A protein proton pump uses ATP to pump protons against the concentration gradient Protons want to go back in so they go down the concentration gradient using facilitated diffusion in a Sucrose cotransporterEnergy associated with the proton gradient help protons and sucrose move across the membrane

Sodium-
Potassium
Pump

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The Sodium-Potassium Pump: A specific case of Active Transport This pump is present in all animal cellsThis ensures sodium is lower on the inside and more on the outside. This also ensures the potassium is higher on the inside and lower on the outside.

Voltage Difference

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Due to these pumps, a voltage difference is made Outside the membrane is slightly positive (some more Na+ ions)Inside the membrane is slightly negative (some more K+ ions, think of salty banana)

Ion Channels

Ungated

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Always Open

Stretch-gated

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Also known as sense stretched, open when membrane is mechanically deformed

Ligand-gated

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Open and close when a neurotransmitter binds to channel

Voltage-gated

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Open and clsoe in response to changes in membrane potential

High
Permeability

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High permeability Small nonpolar molecules can cross through on their ownSmall uncharged polar molecules like water and glycerol

Low
Permeability

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Large, uncharged molecules such as glucose cannot cross on its onAs well as ions like Na+ and K+

Diffusion

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Solvent moving from low solute concentration to higher solute concentration. Desire to create an equilibrium.

Animal Tonicity

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Hypotonic: Excess water is in the cell and the cell is lysed and explodes. This is due to high solute concentration within the cell and water rushing inside. Isotonic: Water is both leaving and entering the cell in equilibrium. This is also called normal Hypertonic: High solute concentration outside the cell causes water to rush outside the cell. Cell gets shriveled up, this usually causes cell death.

Plant Tonicity

Facilitated
Diffusion

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Facilitated Diffusion is passive transport aided by channel proteins. However, no ATP is required for this type of transport

Types of Receptors

Intracellular

Membrane-bound

Extracellular

Concept Map 3

Transcription

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DNA --> mRNA

Prokaryotes

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Occurs in cytoplasm Transcription and Translation are coupled = happens immediately

RNA Polymerase

r

Enzyme used to make mRNA during Transcription in Prokaryotes

Eukaryotes

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Occurs in the nucleus

Transcription

Initiation

Transcription Factors

r

Binds to the promoter FIRST to help RNA Polymerase II bind next

RNA Polymerase II

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ENZYME: binds to the promoter AFTER Transcription Factors bind = Transcription Initiation ComplexUnwinds DNA and starts RNA synthesis

TATA Box

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Section on the promoter for Transcription in Eukaryotes

Elongation

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RNA Polymerase II moves downstream of DNAAdds to the 3' end using dehydration reactions = double helix

Termination

5' Cap

3' Poly A Tail

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Added by Poly A PolymeraseIncreases mRNA stability

RNA Processing

Spliceosome

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ENZYME: cuts introns, joins extrons to form mature mRNAKEEPS 5' CAP AND 3' POLY A TAIL

Alternative Splicing

r

Removing different introns = different mRNA combinations = different proteins

Gene Regulation

r

Aims to control expression at earliest stage - usually at Transcription

Eukaryotes

DCE

r

Distal Control Elements/ENHANCERS Away from promoter

Specific Factors

Repressors

r

Lowers transcription to basal/backgroundMeets mediator proteins during bending

Activators

r

Raises transcription above basal levelsMeets mediator proteins during bending

Promoter

r

TATA box Where RNA Polymerase II binds during bending to control gene expression

PCE

r

Proximal Control Element Closest to promoter

General Factors

Prokaryotes

Operon

r

Regulated expression

Structural Genes

Lac Y

r

Permease Membrane Protein that takes in Lactose

Lac A

r

Transacetylase Adds acetyl group

Lac Z

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Beta-Galactosidase Breaks Glycosidic linkage of Lactose to form Glucose and Galactose

Operator

r

No lactose = Repressor Protein binds here to turn OFF

Promoter

Lac Operon

r

GOAL = Break down Lactose --> GlucoseBoth positive AND negative regulation

No Lactose

r

OPERON OFF - NEGATIVE REGULATIONRepressor protein bind OPERATOR = blocks RNA Polymerase from binding

Lactose Present

r

OPERON ON - POSITIVE REGULATION Repressor protein binds LACTOSE Needs activator

CAP

r

Activated by cAMP (Adenyl Cyclase uses ATP) Binds to Promoter to help RNA Polymerase bind

Lactose & Glucose Present

r

OPERON OFFGlucose = Adenyl Cyclase INHIBITOR Inhibitor = blocks cAMP product = CAP cannot be activated = RNA Polymerase cannot bind to Promoter

Lac I

r

Constitutive (Continuous) expression

Repressor Protein

Regulation

Positive

r

Activator attached = Transcription occursActivator unattached = Transcription does not occur

Negative

r

Repressor attached = Transcription does not occurRepressor unattached = Transcription occurs

DNA Replication

Enzymes

Helicase

r

Function: Unwinds the double helix by breaking hydrogen bonds between base pairs, creating the replication fork.Interaction: Opens the DNA so other enzymes can access the strands.

SSB Proteins

r

Function: Stabilize the unwound DNA strands, preventing them from reannealing or being degraded.Interaction: Coat the strands to keep them separated.

Topoisomerase

r

Function: Relieves supercoiling and torsional strain ahead of the replication fork. Basically Untangles the DNA upstream Interaction: Works upstream of helicase to ensure smooth unwinding.

Primase

r

Function: Synthesizes a short RNA primer to provide a starting point for DNA polymerase.Interaction: Adds RNA primers for polymerase to extend.

DNA Polymerase III

r

Function: Adds nucleotides to the 3' end of the growing DNA strand, using the template strand for complementary base pairing.Interaction: Requires RNA primers; synthesizes the leading strand continuously and the lagging strand discontinuously (Okazaki fragments).

DNA Ligase

r

Function: Joins Okazaki fragments on the lagging strand by sealing nicks in the sugar-phosphate backbone.Interaction: Follows DNA polymerase to finalize the lagging strand.

Exonuclease

r

Function: Removes incorrect nucleotides during replication to ensure fidelity.Interaction: Built into DNA polymerase as a proofreading mechanism.

Process Overview

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Process OverviewHelicase unwinds the DNA, and SSBs stabilize the unwound strands.Topoisomerase relieves tension.Primase lays down primers.DNA polymerase III synthesizes the leading strand continuously and the lagging strand in fragments (Okazaki fragments).DNA polymerase I removes primers and fills with DNALigase seals any remaining nicks to finalize the strand.

Initiation

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Initiation: Helicase unwinds the DNA, primase lays down RNA primers.

Elongation

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Elongation: DNA polymerase synthesizes new strands (leading and lagging).

Termination

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Termination: DNA ligase seals fragments; proofreading corrects errors.

DNA Mutations

Types of Mutations

Silent

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Definition: Alters a nucleotide but does not change the amino acid sequence due to the redundancy of the genetic code.Consequence: Usually no functional impact on the protein. Hence the word "silent". This happens because the codon wheel has multiple inputs for the same amino acid.

Nonsense

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Definition: Changes a codon to a premature stop codon, leading to failed protein synthesis.Consequence: Typically results in nonfunctional proteins or severe loss of function. Also can cause very short proteins

Missense

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Definition: Alters a codon, resulting in a different amino acid being incorporated into the protein.Consequence: Varies from benign to severe, depending on the location and nature of the amino acid change.Example in RNA TranscriptionCAU -> HisMissense mutation that would change it to CAG -> Gln

Frameshift

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Definition: Insertion or deletion of nucleotides (not in multiples of three), shifting the reading frame of the genetic code.Consequence: Alters all downstream codons, usually leading to nonfunctional proteins.

Mutation Sequence &
Consequences

How it Occurs

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Spontaneous: Errors during DNA replication not caught by proofreading mechanisms.Induced: Exposure to mutagens (e.g., UV radiation, chemicals, or carcinogens) damages DNA. Dont smoke cigarettes! This is one of the most common carcinogens!

Most Dangerous

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Frameshift and Nonsense Mutations are generally the most harmful because they severely disrupt the protein’s structure and function.Missense Mutations can also be dangerous if they affect a critical region of the protein, such as an active site.Ironically, I originally wanted to study more into the consequences of Missense mutations and their effects on PrP gene. Prions are an interesting disease that effects proteins and their structure. This basically causes a protein version of cancer. There is no cure for prion diseases. Commonly this will happen in the brain and the misfolded protein will cause other proteins to fold too

DNA Structure

Single Strand

Double Stranded DNA

Adenine, Cytosine, Guanine, and Thymine

(A and G)

(T and C)

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Uracil is also a pyrimidine, but only in RNA.

Double Helix Structure

Semi-conservative replication

Messleson and Stahl Experiment

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The experiment was to use bacterial cells and extract DNA from those cells to predict band distribution. The cells were grown in Nitrogen-15 (high density) combined with CsCl and were spun in a centrifuge for 20 minutes for the first round of replication. The bacteria was then transferred and grown in Nitrogen-14 (normal density) with CsCl and were spun in a centrifuge for 20 minutes for the second round of replication. The experiment concluded that DNA replication was semi-conservative.

Sugar-Phosphate backbone from 5' to 3'

Nitrogenous Bases

Translation

Codons

Anti-Codons

tRNA with Amino Acid

RNA Processing

pre-mRNA

Introns and Exons

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Introns are non-coding sequence regions that are removed in RNA splicing.Exons are genetic coding regions that are combined into one large region for mRNA after RNA splicing.

RNA Splicing

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Spliceosomes can be used to make cuts in pre-mRNA to extract introns to combine exons.

mRNA

Alternative RNA Splicing

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Sometimes mRNA doesn't need all the exons in the sequence, so introns can be used to extract parts of exons in the sequence to code for different proteins. For example, if there are 7 exons in the chromosomal DNA sequence, but only exons 1, 3, 4, 5, 7 are needed for protein A, then spliceosomes will reduce the mRNA sequence to code for protein A after translation is complete.

5' cap

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A modified guanine with three phosphate groups is attached to the 5' end of pre-mRNA.

poly-A tail

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About 50 to 250 adenine nucleotides are added to the 3' end

Ribosome (rRNA)

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Composed of proteins and RNA. Ribosomes (prokaryotic 70S and eukaryotic 80S) have two subunits: large (50S prokaryotic and 60S eukaryotic) and small (30S prokaryotic and 40S eukaryotic) that's about 52 proteins, if prokaryotic, or about 78 proteins, if eukaryotic, attached to mRNA for translation.

Large Subunit

A site

Peptidyl Transferase

Polypeptide chain formed

P site

E site

tRNA exits ribosome

Release factor

Termination

Free polypeptide

Polypeptide chain forms to form the protein signaled

Newly formed protein is transferred to the rough ER to refine protein for pathway

Rough ER

Golgi Apparatus

Plasma Membrane

Secretion

Membrane Protein

Types of Secreted Proteins

Peptide Hormones (Insulin)

Extracellular Matrix Proteins (Collagen)

Milk Proteins (Casein)

Digestive Enzymes (Amylase)

Serum Proteins (Albumin)

Lysosomes

Back to ER

Extracellular Matrix (Eukaryotes Only)

Protein Sorting

Lysosome

Release factor dissociates the ribosome and mRNA is released

Small Subunit

Glycoprotein

Tags bind to cytosol receptors

Protein transports back to Lysosome

Protein transports back to Golgi Apparatus

Proteins transport back to Rough ER

Protein ready for secretion

Photosynthesis

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6CO2 + 6 H2O + Energy --> C6H12O6 + 6O2H2O is oxidized CO2 is reduced GOAL= Make sugar for energy

Light Reactions

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Occurs in Thylakoid of CytoplasmMakes NADPH Electron Carrier

Linear Electron Flow

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PRODUCTS = ATP, O2, H+, NADPH Electron CarrierATP goes against gradient in Thylakoid (High H+, Low pH) Down gradient through ATP Synthase into Stroma (Low H+, High pH) = Photophosphorylation Uses PS II (P6800) and PS I (P700)

Cyclic Electron Flow

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PRODUCTS = ATPOccurs ONLY when NADPH is in excessONLY uses PS I (P700)ELECTRON TRANSPORT CHAIN

Photorespiration Adaptations

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ENZYME = Pep Carboxylase Photorespiration interferes with Carbon Fixation = adaptationsRubisco prefers O2 > CO2 = releases CO2 = blocks photosynthesis = NO ATP/Sugar

CAM Plants

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DIFFERENT TIME OF DAY Night: CO2 Fixation, Stromata Open Day: Calvin Cycle

C4 Plants

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DIFFERENT CELLS Mesophyll = CO2 Fixation Bundle Sheath Cell = Calvin Cycle

Parts

Chloroplast

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Site of PhotosynthesisFound in Mesophyll (interior tissue of leaves)

Stromata

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CO2 IN, O2 OUT

Chlorophyll

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Light harvesting pigment

Calcin Cycle

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Occurs in Stroma Whole Cycle = 9 ATP, 6 NADPH, produces 1 G3P1 Glucose Molecule = 3 CO2, 18 ATP, 12 NADPH Makes ATP

Carbon Fixation

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CO2 + RUBP (use Rubisco - ENZYME) = 6C (unstable) = 3C 6 ATP --> 6 ADP = 6 1-3 Bisphosphoglycerate

Regeneration

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5 G3P from Reduction, 3 ATP --> 3 ADP = 3 RuBP for Phase 1

Reduction

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6 NADPH --> 6 NADP+, 6Pi = 6 G3P --> exports 1 (PRODUCT)