BIO 311C
Topic 2:
Membranes, Energy, and
Cell Communication
Cell Signaling/ Communication
Long-distance signaling
Seen in hormonal signaling
Local Signaling
Seen in paracrine and synaptic signaling
Physical contact
Communications through gap or plasmodesmata junctions. Physical contact communication can also occur through surface protein and binding of the surface proteins.
Intracellular Receptors
Ligand: Hydrophobic or nonpolar molecule
Ligand will pass through the membrane
Ligand will bond to a receptor protein in the cytoplasm
Hormone-receptor complex will enter the nucleus and binds to specific genes
Bound protein is a transcription factor (controls gene expression) and regulates the transcription of mRNA
mRNA is translated
Thyroid and steroid hormones
Membrane Receptors
Ligand (First Messenger): Hydrophilic
Second messenger
Location: inside the cell
Location: Cell membrane
Ion channel receptor
Ligand binds to a ligand-gated channel receptor
Ligand-gated channel receptor will open and specific ions will flow through the channel
The ions flowing in will change the ion concentration within the cell.
Pertaining to the nervous system: action potential due to the change of voltage across the cellular membrane.
The ligand will unbind from receptor which then closes the ligand-gated ion channel
Tyrosine kinase receptor
dimerize once ligand binds to each of the tyrosine polypeptides
autophosphorylation - activation of the kinase function to transfer phosphate from ATP to the other tyrosine polypeptide
creates the tyrosine-kinase receptor
activated tyrosine-kinase receptor creates a cellular response
Used for cell division
G-protein linked receptor
Reception: Ligand binds to the G protein-coupled receptor. This in turn causes a change of shape of the GPCR for the G-protein to bind to it. Now, GDP converts to GTP to bind to G-protein and activate G-protein.
Transduction: In turn causes a change of shape of the GPCR for the G-protein to bind to it. Now, GDP converts to GTP to bind to G-protein and activate G-protein. , the G-protein detaches from the GPCR and binds to Adenylyl Cyclase. The Adenylyl Cyclase then turns ATP to cAMP (the second messenger).
Transduction (amplifying): cAMP activates Protein Kinase A to transfer ATP to activate another kinases
Cellular response : Will different due to the different GPCR and the cells.
phosphorylation cascade: kinases that phosphorylate and activate each other.
Dephosphorylation: The use of phosphates to inactivate kinases, by removing phosphate groups.
G-protein switch: Phosphodiesterase converts cAMP to AMP. Due to the conversation of cAMP to AMP, there is no secondary messenger to continue in the signaling pathway.
Signaling molecules that use GPCR: epinephrine, hormones, and neurotransmitters
Metabolism
Catablic Pathways
Anabolic Pathways
Cellular Respiration & Photosynthesis
Topic 1:
Chemical Bonds, Cell
Structure and Function
Prokaryotes
Structure
Shape
Coccus
Spherical Shape
Basillus
Rod Shape
Spirilla
Spiral Shape
Cell Surface Structures
Cell Wall
Shape
Cell
Peptidoglycan
Gram Positive
Thick Layer of Peptidoglycan
Gram Negative
Thin Layer of peptidoglycan
Fimbriae & Pili
Attachment to surfaces
Bacterial Mating
Flagella
Movement
Bacterial Flagella
3 Main Parts
Motor
Hook
Filament
Powered by H+ Flow
Archaeal Flagella
Powered by ATP
Capsule & Slime layers
Resistance
Phagocytosis
Adherence
Plasma membrane
Permeable Barrier
Functions
Protection from environment
Waste Transport
Nutrient Transport
Internal Cell Structures
Nucleiod
contains DNA
Ribosomes
protein synthesis
Periplasmic Space
Contains hydrolytic enzymes and binding proteins
nutrient processing and uptake
Classifications
Archea
Extremophiles
Extreme Halophiles
Highly Saline Environments
Extreme Thermophiles
Extreme Temperaters
Methanogens
Swamps
Produce methane as a waste product
Bacteria
Topic 3:
DNA Structure, Replication,
Regulation, and Expression
DNA Structure & Replication
3 experiments
Griffith
Injected mice with
S. pneumoniae
"smooth"
presence of
capsule
Pathogenic
R. pneumoniae
"rough"
no capsule
Nonpathogenic
Experiment
Living S
Mouse dies
S. strain found to be
pathogenic
Living R
Mouse healthy
R. strain found to be
nonpathogenic
Heat-killed S
Mouse healthy
Heat-killed S
& Living R
Mouse dies
S. components entered
live R. and changed the
genetic makeup of R to S
Hershey & Chase
One tube of Radioactive
Phosphorus (32P)
Labeled DNA
Mixed
Shook tube to release
bacteriophages from
bacterial surface
Centrifuged
Recovered radioactivity
inside bacterial cells
One tube of Radioactive
Sulfur (35S)
Labeled Proteins
Mixed
Shook tube to release
bacteriophages from
bacterial surface
Centrifuged
Asked what was the component
that was injected by bacteriophages
inside bacterial cells, DNA or Protein?
Determined DNA was injected
Determined DNA
carried genes
Messleson &
Stahl
Bacteria in 15N
"Heavy"
Bacteria in 14N
"Light"
Found from
density bands that
DNA replicates
semiconservatively
DNA structure
Chargaff's Rule
Adenine=
Thymine
Guanine=
Cytosine
A+G=
T+C
Sugar phosphate
backbone
Phosphate group
Sugar
Nitrogenous bases
Thymine (T)
Guanine (G)
Cytosine (C)
Adenine (A)
Nuceotide
Phosphate Group
Sugar
Nitrogenous base
Bond connecting
each nucleotide=
phosphodiester
bond
Double Stranded
Helix
Purine+Pyrimidine
Adenine(A)+Thymine(T)
Guanine(G)+Cytosine(C)
Complementary base pairing
DNA Replication
3 Models of DNA Replication
Conservative
Two parent strands
reassociate after
acting as template
strands and restore the
parental double helix
First Replication
One parent helix
One new helix
Second Replication
3 daughter helices
One parent helix
Semiconservative
Two parent strands
separate and each
functions as a template
for a new complementary
strand
First Replication
Two helix
Each helix contains
one parent strand
and one new strand
Second Replication
2 new complementary
helices
2 helices
Contain one parental
strand and one new
strand
Dispersive
Each strand of both
daughter molecules
contains a mixture of old
and new synthesized DNA
First Replication
2 helices
Contain pieces of
parental strand
and pieces of new
DNA
Second Replication
4 helices
Contain pieces of
parental strand
and pieces of new
DNA
Replication process
Needs origin of
replication (ORI)
Enzymes
Helicase
Unwinds parental
double helix at
replication forks
Single Strand
Binding (SSB)
Binds and stabilizes
single stranded DNA
and prevents it from
rebinding
Topoisomerase
Relieves overwinding strain
ahead of replication forks
by rejoining DNA strands
Primase
Makes RNA primers
at 5' end of leading strands
and each Okazaki fragment
DNA Polymerase
III
Synthesizes new DNA
5' to 3' by using the
parental DNA as a template
Nucleotides connect
through phosphodiester
bonds using
dehydration reaction
DNA Polymerase I
Removes RNA
nucleotides and replaces
them with DNA nucleotides
DNA Ligase
Joins DNA together
Occurs in one direction
5' to 3'
Transcription
Prokaryotes
Occurs in the Cytoplasm
(Coupled with Translation, mRNA is made and immediately translated)
Stages of Transcription
Initiation
- The beginning of transcription that occurs when the enzyme RNA polymerase binds to the promoter. (RNA Polymerase)
RNA Polymerase
- The RNA polymerase seen in prokaryotes. (Makes new strand of mRNA in 5' to 3' direction)
Elongation
- This step follows initiation as RNA polymerase moves downstream, unwinding the DNA and elongating the RNA transcript in the direction of 5' to 3'. (Uses condensation/ dehydration reactions)
Termination
-This step occurs when the RNA transcript is released, and the polymerase detaches from the DNA. This happens once the RNA polymerase reaches the termination site on the DNA.
Location of Transcription
Template Strand
- The DNA strand that is used to form the new RNA strand. (Template strand is in the 3' to 5' direction because transcription occurs in the 5' to 3' direction.)
Transcription Start Point
- The nucleotide in DNA where transcription starts.
Upstream
- To the left of the transcription start site, nucleotides are numbered by negative numbers.
Promoter
- Region on the DNA upstream of the start site where RNA polymerases bind to.
Downstream
- To the right of the transcription start site, nucleotides are numbered by positive numbers.
Eukaryotes
Occurs in the Nucleus
(Not coupled with Translation, translation occurs in the cytoplasm.)
Stages of Transcription
Initiation
- The beginning of transcription that occurs when the enzyme RNA polymerase binds to the promoter. (RNA Polymerase II)
TATA Box
- A eukaryotic promoter commonly includes a TATA box, which is a nucleotide sequence containing TATA that is about 25 nucleotides upstream from the transcription start point.
Transcription Factors
- In eukaryotes, the addition of these proteins is required in order for RNA polymerase II to bind to the promoter. One recognizes the TATA box and binds to the promoter.
RNA Polymerase II
- The RNA polymerase seen in eukaryotes which is used to produce pre mRNA, snRNA, and micro RNA. (Makes new strand of mRNA in 5' to 3' direction)
Transcription Initiation Complex
- Additional transcription factors bind to the DNA along with RNA polymerase II, forming this complex. RNA synthesis can now begin at the start point on the template strand.
Elongation
- This step follows initiation as the transcription initiation complex moves downstream, unwinding the DNA and elongating the RNA transcript in the direction of 5' to 3'. (Uses condensation/ dehydration reactions)
Termination
- This step occurs in eukaryotes differently as an AAUAAA sequence signals the cell to make a cut in the newly formed pre mRNA and release it from the DNA.
Ribonuclease
- The enzyme that makes the cleavage to form the pre-mRNA.
pre-mRNA Processing
5' Cap
- A modified guanine (G) nucleotide added to the 5' end of the pre-mRNA that will be used for translation.
Poly A Tail
- A tail of 100-200 A's that is added to the 3' end of pre-mRNA, near the AAUAAA sequence. This poly A tail helps with the stability of the mRNA.
Poly A Polymerase
- The enzyme that adds the poly A tail to the pre-mRNA. (Requires ATP)
RNA Splicing
Introns
- Non-coding sequences that are removed during RNA splicing.
Spliceosomes
- Complexes of RNA and proteins that bind junctions of the introns and makes cuts to release introns from the DNA. The exons are then joined together.
Alternative Splicing
- Due to the presence of introns, different combinations of exons can be generated through the removal of different introns to form different mRNAs.
Exons
- Coding sequences of mRNA that are used to encode proteins.
Translation
Gene Regulation
Regulating which genes are expressed and when they are expressed
Eukaryotes
DNA material present in the nucleus
DNA wraps around histones to form nucleosomes and further coil into the chromatids of chromosomes.
Transcription
Transcription Factors
Specific
Changes level of transcription by increasing or decreasing
Repressor
Activator
Distal control elements
upstream or downstream of DNA
proximity to the gene they regulate can vary
Enhancers
If activator was to bind to enhancers: The activator proteins are brought to be near the promoter by a DNA-bending protein. With this the activators then can also bind to more (mediator) proteins that form an initiation complex. Through these interactions and the development of the complex, it assists RNA polymerase II to bind to the promoter in order to increase the level of transcription.
If repressors were to bind to an enhancer: The main goal of a repressor is to block or decrease the probability the RNA polymerase II can bind to the promoter. By decreasing the effectiveness, it decreases levels of transcription of the pre-mRNA
Combinatorial control of gene expression
Liver and cell cells expressing different levels of the albumin and crystallin genes.
General
Bring transcription levels to background or basal (meaning lower)
Proximal control elements
Regulation can also occur at RNA processing, translation, and protein activity or modifications.
Prokaryotes
Only at transcription level
Examples seen through the Lac Operon
decreases gene expression to a basal level
Lac operon with no lactose present: Repressor is bound to the operator thus lacZ, lacY, and lacA are not transcribed for Beta-glactosidase, permease, and transacetylase. Operon is off as the activated repressor blocks the binding of the RNA polymerase to the promoter.
Lac operon with glucose present, regardless if there is lactose: Glucose blocks the function of adenylyl cyclase, meaning no cAMP can be generated. Due to this, CAP is not activated to then also activate RNAP. If RNAP is not activated, it cannot bind to the promoter to bring about the high level of transcription. This means the operon is off as it cannot transcribe its structural genes (lacZ, lacY, and lacA).
increases gene expression level
Lactose present: The lac repressor from LacI (which is constitutively expressed, meaning continuously expressed) will bind to the lactose instead of the operator. RNAP is activated by cAP (which is activated by cAMP, a product of adenylyl cyclase) and binds to the promoter to increase the level of transcription for proteins that will break down lactose to a high level. The operon is on.
Negative regulation repressors while positive regulation is associated with activators
operons (genes), operators (sequences of DNA), activators/repressors, promoters, mRNA, and proteins
The genes are grouped in operons. Several sequences of DNA are operators that can turn on or off the gene expression.
Bonds
Intermolecular (between)
Van Der Waals
More apparent in nonpolar molecules
Hydrophobic Interactions
Tertiary structure of proteins
Phospholipid bilayer/membrane
Dipole-dipole
Strong interactions between polar molecules
Hydrogen Bonds (H to O, N, or F)
Complementary base pairing
Water molecules
Water properties
Secondary structure of proteins
Dipole-ion
Between ions and polar molecules
Intramolecular (within)
Covalent
Disulfide Bonds
Tertiary structure of proteins:
Cysteine (R-group)
Glycosidic Bond/Linkage
Monosaccharides to form polysaccharides
Beta glycosidic linkages
Cellulose
Alpha glycosidic linkages
Starch, Dextran, Glycogen,
Amylose, and Amylopectin
Polar
Slight/ partial charges
Nonpolar
Non-charged
Peptide Bonds
Between the amino and carboxyl group
Primary structure of protein
Phosphodiester Linkage
Between the phosphate group and sugar of 2 nucleotides
Sugar phosphate backbone
Ester Linkage
bond between a glycerol and fatty acid
Hydrocarbon chains
Double Covalent: Unsaturated Fats
Ionic
Ionic Compounds
Acidic/Basic R-groups in
Tertiary and Quaternary structures of proteins
Ether linkages
Membranes of Archaea
(branched)
Macromolecules
Hydrogen, Oxygen, Nitrogen, Carbon, Phosphorus
Dehydration Synthesis
Removal of H2O
Forms Glycosidic Linkage
Forms Ester bonds
Forms Phosphodiester Bond
Forms Peptide Bond
Glucose
β Beta Glucose (OH on top)
α Alpha Glucose (OH on bottom)
Fructose
Sucrose
Triglycerides
Phospholipids
Cholesterol
Saturated
Unsaturated
Four Rings
LDL
HDL
DNA
RNA
Deoxyribose
Ribose
Nucleobase
Solid @room temp.
Liquid @room temp.
No double bonds
Has double bonds (kinks)
Cis
Trans
Hydrogen atoms are on the same side
Hydrogen atoms are across
Bonds phosphate group
With sugar
Amino Acid
Amine Group
Carboxyl Group
Hydrogen
R-Group
Polypeptide
Primary Structure
Secondary Structure
Single strand of Amino acids
Tertiary Strucrure
Quaternary Structure
Form Structures
H bonds form between the polypeptides
Beta Pleaded Sheet
R-Groups Interact
Alpha Helix
3-D Shape
Multiple 3° with R-Group Interactions
Multiple Structures
Function
Realease Energy
Consume Energy
Energy
Laws Of Thermodynamics
Energy cannot be created or destroyed
Energy trasnfer increases entropy
Gibbs Free Energy
Equation: ΔG=ΔH-TΔS
G=Gibbs
H=Enthalpy
S=Dissorder
Δ=Change
T=Temperature (kelvin)
ΔG can be
Endergonic
Exergonic
Realease of free energy (-#)
Absorb of free enery (+#)
Reactants have more free energy
Products have more free energy
ΔG<0
ΔG>0
Reaction can occur Spontaneously
Reaction can cannot occur spontaneously
ΔG=0
System is at equillibrium
Make Coupler Reactions
Reactions Have
Enzymes
Lower activation Energy
Speeds Up Reactions
ΔG is not affected
Enzyme/Substrate
Denatures by
High Temperatures
Change of preffered pH
Inhibition
Competitive
Noncompetive
Allosteric Regulation
Cooperativity
Feedback
mimics substrate
competes for active site
binds away from active site
alters shape pf enzyme
inhibitor or activator
Binds to protein at one site
Affects proteins function at another site
Binds to one active site
Locks all subunits
End product is inhibitor
Pathway is halted
mRNA
tRNA
Codon
Anti-codon
Initiation
Elongation
Termination
small ribosome bind tRNA and mRNA from 5'
tRNA is in P site
tRNA carries correct amino acid
Amino acid goes to the A site
Peptidyl Transferase
Forms peptide bonds between amino acids
mRNA is read from 5' --> 3'
amino acids added from N to C
tRNA moves when P site is empty
tRNA moves to E site to be released
A new tRNA comes to the A site
Release factor
empties A site and causes everything to fall apart
Protein is released in the ER lumen.
Signal peptidase
Enzyme that cleaves the signal peptide
Protein is now in the ER
Protein gets shipped out through vesicles and then fuze onto the first phase of Golgi
Protein has different destinations
Secretion
Membrane Protein
Lysosomes
Back to ER
Eukaryotes
Intracellular Organelles
Ribosomes
- Comprised of ribosomal RNA and protein. Produces proteins
Free Ribosomes
- Ribosomes suspended in the cytosol
Bound Ribosomes
- Ribosomes that are on the outside of the ER
Nucleus
- Storage site for DNA
Chromosome
- One long DNA molecule that forms when a cell is prepared to divide (CONDENSED Chromatin)
Chromatin
- Material consisting of DNA and histone proteins
Nucleolus
- Site of ribosomal RNA synthesis
Nuclear Envelope
- Double membrane enclosing the nucleus; continuous with the ER
Nuclear Pores
- Small openings lined with porin proteins that assist in transport
Lamina
- Protein filament meshwork that lines the inner surface of nuclear envelope and keeps its structure
Endomembrane System
- Regulates protein traffic and performs metabolic functions
Lysosomes
- Organelles packed with enzymes that promote the hydrolysis of biological molecules
Phagocytosis
- Extending a cell's membrane to engulf a foreign cell or food particle
Autophagy
- A process that uses hydrolysis enzymes to recycle cell's own organic material
Vacuoles
- Large vesicles that are meant to store substances
Food Vacuoles
- Formed when cells engulf food or other particles
Contractile Vacuoles
- Pump excess water out of cells
Central Vacuoles
- Found in plant cells and serves as a repository for inorganic ions and water
Endoplasmic Reticulum
Rough ER
- Secretes glycoproteins, distributes transport vesicles, and is considered the membrane factory of the cell
Smooth ER
- Synthesizes lipids, metabolizes carbohydrates, detoxifies drugs and poisons, and stores calcium ions
Golgi Apparatus
- Modifies products of the ER and moves them to their final destination
Trans Face
- Releases cargo after making changes
Cis Face
- Receives cargo shipped out by ER
Plasma Membrane
- To protect the cell from the surrounding environment and regulate the materials that enter and exit from the cell
Endosymbiont Theory
- Origins of mitochondria and chloroplasts. Prokaryotic (non-photosynthetic and photosynthetic) cells engulfed by eukaryotic cells and formed symbiotic relationships with them. (Energy)
Mitochondria
- A double membrane organelle that produces ATP through cellular respiration
Cristae
- Folds within the mitochondria
Intermembrane Space
- Space between inner and outer membranes
Matrix
- Space inside the inner membrane where DNA is
Chloroplast
- A double membrane organelle that synthesizes food through photosynthesis
Granum
- Stack of thylakoids
Thylakoid
- Membranous sac
Stroma
- Internal fluid
Peroxisomes
- A single membrane organelle that is packed with enzymes that produces various metabolic functions like extracting hydrogen from certain molecules and adding them to oxygen to form hydrogen peroxide, which is then turned to water.
The Cytoskeleton
Microtubules
- Thickest of the three, hollow rods made of a protein called tubulin. Grow in length by adding tubulin dimers; very dynamic
Functions:
- Maintenance of Cell Shape
- Cell Motility
- Chromosomal Movement in Cell Division
- Organelle Movement
Flagella
- Mobility structure that is limited to one or few per cell. (Cell motility, composed of microtubules (9 doublets surrounding 2 microtubules))
Cilia
- Mobility structure that occurs in large numbers on cell surface. (Cell motility, composed of microtubules (9 doublets surrounding 2 microtubules))
Centrosomes
- "Microtubule organizing center" that helps with cell division. (Composed of 9 sets of triplet microtubules)
Intermediate Fibers
- Intermediate diameter compared to the three, very diverse and made up of different proteins. These structures are more permanent (Ex: Nuclear Lamina)
Function:
- Maintenance of cell shape
- Anchorage of nucleus and certain organelles
- Nuclear Lamina
Microfilaments/Actin Fibers
- Thinnest of the three, two thin intertwined strands of actin
Function:
- Maintenance of Cell Shape
- Muscle Contraction
- Cellular Movement/ Amoeboid Movement
- Cytoplasmic Streaming
Extracellular Components
Cell Junctions
Plasmodesmata
- Channels present between plant cells that go through cell walls, allowing the transfer of water and other nutrients (Plant)
Tight Junctions
- Membranes of adjacent cells tightly connected with proteins preventing the movement of any fluid or substance (Animal)
Desmosomes
- Connections between cells through proteins that allow some substances to go between cells (Animal)
Gap Junctions
- Allows everthing to move between cells (Animal)
Cell Wall
- Provides structure for plant cell
Primary Cell Wall
- Relatively thin and flexible
Middle Lamella
- Thin layer between the primary walls of adjacent cells
Secondary Cell Wall
- (In some cells) added between the plasma membrane and primary cell wall
Extracellular Matrix
- Comprises of a lot of different proteins and is a network that provides structure for animal cells
Plant Cell Structures
Animal Cell Structures
Cell Membrane and Structure
Structure
Fluid Mosaic Model
- Describes phospholipids as a fluid component of the membrane while different types of proteins (mosaic) are present in the bilyaer.
Phospholipids
- An amphipathic molecule that is contains a hydrophilic head and two hydrophobic tails. Hydrophilic heads are positioned to be in contact with extracellular and intracellular fluids while hydrophobic tails orient themselves inside the bilayer.
Membrane Fluidity
Temperature
- Temperature affects membrane fluidity. Above specific phase transition temperature, the lipid is in a liquid crystalline phase and below the lipid is in a gel phase.
Cholesterol
- Cholesterol also affects membrane fluidity. Its presence between phospholipids reduces movement at moderate temperatures and prevents phospholipids from packing tightly at low temperatures.
Hydrocarbon Tails
- The type of hydrocarbon tails affects membrane fluidity. Unsaturated fatty acids allow the membrane to more freely and saturated fatty acids pack tightly so the membrane cannot move as much.
Membrane Proteins
Peripheral Proteins
- Proteins that are anchored to the membrane.
Integral Proteins
- Proteins that are partially or fully inserted into the membrane.
Transmembrane Proteins
- Proteins spanning the entire membrane. N-terminus on extracellular side and C-terminus on intracellular side.
Function
Functions of Membrane Proteins
- Transport
- Enzymatic Activity
- Signal Transduction
- Cell-Cell Recognition
- Intercellular Joining
- Attachment to Cytoskeleton and ECM
Selective Permeability
- The ability for a cell membrane to control which molecules can pass through it.
Passive Transport
- Membrane transport that does not require energy and utilizes a concentration gradient to exchange small nonpolar and small uncharged polar molecules across the membrane. (With Concentration Gradient)
Osmosis
- The diffusion of free water across a selectively permeable membrane, going from an area of higher solute concentration to an area of lower solute concentration.
Tonicity
- The ability of a surrounding solution to cause a cell to gain or lose water.
Animal Cells
- Due to no cell wall, animal cells fare best in isotonic environments unless they have special adaptations.
Hypertonic Solution
- Solute concentration is greater than that inside the cell; cell loses water. (Shriveled)
Isotonic Solution
- Solute concentration is the same as the inside of the cell, no net water movement. (Normal)
Hypotonic Solution
- Solute concentration is less than that inside the cell; cell gains water. (Lysed)
Plant Cells
- Cell walls in plant cells help maintain water balance.
Hypertonic Solution
- Solute concentration is greater than that inside the cell; cell loses water. (Plasmolyzed)
Isotonic Solution
- Solute concentration is the same as the inside of the cell, no net water movement. (Flaccid)
Hypotonic Solution
- Solute concentration is less than that inside the cell; cell gains water. (Turgid)
Diffusion
- The tendency for molecules of any substance to spread out evenly into the available space because of thermal motion, moving from an area of high concentration to an area of low concentration.
Facilitated Diffusion
- Membrane transport that does not require energy but does utilize a transport protein and a concentration gradient to exchange large, uncharged molecules across the membrane. (With Concentration Gradient)
Channel Proteins
- Proteins that provide corridors or channels that allow a specific molecule or ion to cross the membrane
Aquaporin
- A channel protein that is present in the membrane that helps facilitate water through the membrane by use of aqua pores.
Carrier Proteins
- Proteins that undergo a subtle change in shape, alternating between two shapes. The shape change may be triggered by the binding and release of the transported molecule.
Active Transport
- Membrane transport that utilizes energy to move ions against their concentration gradients.
Electrogenic Pump
- A transport protein that helps create a voltage difference across membranes.
Sodium-Potassium Pump
- Typically, the outside of the cell has an abundance of Na+ and the inside of the cell has an abundance of K+, so if the cell needs to take out more Na+ or bring in more K+ it needs to do it against the concentration gradient. For every 3 Na+ transported outside the cell, 2 K+ ions are transported inside. (Requires ATP)
Proton (H+) Pump
- A pump that transports H+ against its concentration gradient. As positive charge leaves the cell, we see a slight negative charge develop inside the cell and a slight positive charge develop outside the cell.
Cotransport
- When active transport of a solute indirectly drives transport of other substances. (Ex: H+/Sucrose Cotransporter)
Bulk Transport
- The use of vesicles to move large molecules such as polysaccharides and proteins in bulk cross the membrane .
Exocytosis
- Transport vesicles migrate to the membrane, fuse with it, and release their contents.
Endocytosis
- Contents collect onto the plasma membrane, and they fuse into a transport vesicle where the contents travel within the cell.
Phagocytosis
- When a cell engulfs large food particles by extending part of its membrane out. The ingested particle is now in a food vacuole where it will fuse with lysosomes and be digested.
Pinocytosis
- When a cell takes in extracellular fluid from outside in vesicles. This allows the cell to take in any dissolved molecules.
Receptor-Mediated Endocytosis
- A very specialized form of pinocytosis that allows the cell to acquire bulk quantities of a specific substance. This can occur due to the presence of receptors on the plasma membrane which allow for the binding of specific solutes.
Cellular Respiration
Stages
Glycolysis
Occurs in cytoplasm
Two Phases
Energy Investment
2 ATP -> 2 ADP +2 Pi
Energy Payoff
4 ADP +4Pi
2 NAD+ +4 electrons +4 H+->
2 NADH +2H+ & 2 Pyruvate + 2 H2O
Net
2 Pyruvate + 2H2O
2 ATP
2 NADH + 2H+
Pyruvate Oxidation
& Citric Acid Cycle
Pyruvate Oxidation
1 Acetyl CoA per pyruvate
Citric Acid Cycle
8 Steps
1 Cycle
1 ATP
3 NADH
1 FADH2
2 Cycles
2 ATP
6 NADH
2 FADH2
Oxidative Phosphorylation
ETC
Transfer of electrons and release
of energy at each step rather than
all at once
Proton Pumps
NADH and FADH2
carry electrons
creates H+ gradient
across the membrane
Chemiosmosis
ATP synthesis
powered by the flow of H+
back across the membrane
ATP synthase
Prokaryotes
Cytoplasm
& Inner face of plasma
membrane
Eukaryotes
Outside and inside the
mitochondria
Chemical Formula
C6H1206 + 6O2 -> 6 H2O + Energy
Glucose becomes oxidized
loses electrons
O2 becomes reduced
gains electrons
ATP yield
1st stage
2 ATP
2nd stage
2 ATP
3rd stage
around 26 or 28 ATP
TOTAL:
30 or 32 ATP
Fermentation
absence of oxygen
Alcohol Fermentation
Glycolysis
2 Pyruvate
2 Ethanol
Lactic Acid Fermentation
Glycolysis
2 Pyruvate
2 Lactate
Photosynthesis
Chemical Formula
6CO2 +6H2O + Light Energy ->
C6H12O6 +6O2
6H2O extracted from
soil
6 O2 released
ENTIRE PROCESS
6CO2+ 18 ATP+12 NADPH +12 H2O->
C6H12O6+18 ADP +18 Pi+12 NADPH
+6O2 +6H2O+ 12 H+
Chloroplasts
cells of mesophyll
interior tissue of the leaf
1 mesophyll contains
30-40 chloroplasts
Stomata
Where CO2 enters
and O2 exits
Microscopic pores
2 Stages
Stage 1
Solar to chemical energy
H2O is split for protons
O2 is released
Photophosphorylation
ATP is generated by adding
a phosphate group to ADP
Stage 2
Calvin Cycle produces sugar
from CO2 with NADPH and ATP
ATP provides energy
NADPH provides electrons to
reduce CO2
Carbon Fixation
CO2 is incorporated into an
organic molecule
Photosystems
Photosystem I
chlorophyll a absorbs
at 680 nm
Photosystem II
chlorophyll a absorbs
at 700 nm
Thylakoid Membrane
Non Cyclic (Linear)
Photosystems I and II
Produces both ATP
and NADPH
Cyclic
Photosystem I
only produces
ATP