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65 Cards in this Set

  • Front
  • Back
Organ Systems
Plasma Membrane Structure
Phospholipid bilayer embedded with proteins and carbohydrates
Passive Transport

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
Active Transport
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
Vesicular Transport
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
Found throughout cytoplasm
-allows for support and movement
What are the 3 kinds of cytoplasm?
microtubules, microfilaments, and intermediate filaments
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
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
-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
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
genetic library of eukaryotic cells

chromatin: DNA and associated proteins

mRNA synthesis

has double membranes and pores
rRNA synthesis-found in ribosomes

Makes up ribosomal units
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
Endoplasmic Reticulum
-continuous with nuclear envelope
-cisternae: internal space
Smooth ER
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
Rough ER
-prep proteins for delivery that are formed on bound ribosomes
-secreted proteins and membrane proteins made by ribosomes and processed by ER
Golgi Apparatus
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
Lysosome Formation
made in rough ER
-enzyme and membrane created in Rough ER

-lysosome membrane isolates disgestive enzyme from rest of cell
Proton Pump
makes inside have low pH of 5
Lysosome enzymes
works best in low pH
hydrolyze proteins, fats, polysaccharides and nucleic acids
What do lysosomes fuse with?
vacuoles to digest food

-recycle damaged organelles

-phagosomes to destroy invaders
lysosome deficent disease
4 classes of signal molecules
1) secreted signals that act locally

2) secreted signals for long distance

3)intracellular signals

4) cell surface signals
Secreted Signals that act locally
a) paracrine signaling- growth factors

b) synaptic signaling- neurotransmitters
Secreted cells for long distance
travels through circulatory system in animals.

for plants: vessels, cell to cell, or diffusion in air
Intracellular Signals
a) cell junctions

ex. gap junctions between animal cells
plasmodesmata between plant cells
Cell surface Signals
a) cell to cell recogniition

ie. blood antigens and antibodies
Cell signaling process


Reception for Cell Signaling
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
Specific types of plasma membrane receptors
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
Intracellular Receptors
-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
Living matter is made up of?
96% is made from C, O, N, H
Out of 92 elements, how many are essential to life?
Types of Bonds
covalent- non polar and polar

ionic- ex: Na+Cl-

hydrogen: only occurs in polar molecules. weak attraction force between dipoles.
Functional Properties of Water
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
increase H+ in solutions
decreases H+ in solutions
resist change in pH of solution

-donate H+ when in excess
-Accept H+ when depleted
What's the pH of Human Blood? And what is it buffered by?
pH 7.4

carbonic acid and bicarbonate

H2CO3--> HCO3- + H+
acid base hydrogen ion
Carbon bonds to what?
carbon based compounds make what?



Factors contributing to molecular diversity
1. large variation of carbon skeleton

2. functional groups that replace H (like hydroxyl, carbonyl, carboxyl, sulfurhydral, amino, and Phosphate)
Carbon based macromolecules
carbohydrates, proteins, nucleic acids are made up of polymers
long molecules built from small similar subunits(monomers) linked by covalent bonds
What are lipids made out of
two or more different subunits.

hydrophobic which means it has a nonpolar covalent bond.
What are the two ways to Form or dissasemble polymers?
Dehydration- loss of water and then it joins

Hydrolysis-addition of water and ten they break apart
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
In what form energy stored in plants and animals?
plants- startch

animals- form of glycogen
What are the forms of Lipids?
Fats, Phospholipids, and Steriods
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
made up of

Glycerol+2 fatty acids+phosphate+choline

phospholipid bilayer
carbon skeleton with four rings and varying functional groups

-ex: cholestrol

-found in membrane
-precursor to testostrome and estrogen
Protein Functions
-enzyme(catalyzes stuff)



-signaling/ transport
Structure of Protein
amino acids-> monomers-> polymers(polypeptides)-> protein
Levels of Proteins
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)
What in the environment is the protein influenced by?
pH, salt, and temperature
What happens to damaged proteins?
-tagged by ubiquitins
-delivered to proteosomes
-proteases chops protein into short peptides for reuse

or chapperone protein comes and folds it
Nucleic Acids Functions
store and trasnmit hereditary information
two rings

Adenine or Guamine for DNA

For RNA it's Uracil
One ring

cyotsine or thymine
How does DNA copy?
1.mRNA synthesis
2.moves out of nucleus
3. protein synthesis with ribosomal subunits
Structure for ATP
3 phosphate+ Ribose+ adenine
when energy goes from high to low
-change in G is less than 0
when energy goes from low to high
-change in G is greater than 0