Catégories : Tous - membrane - proteins

par Chelsi Lam Il y a 7 mois

208

BIO 311C

The fluid mosaic model of cell membranes describes how phospholipids and various proteins create a dynamic structure. Phospholipids have hydrophilic heads and hydrophobic tails, aligning themselves to form a bilayer with heads facing outward towards the extracellular and intracellular fluids.

BIO 311C

Photosynthesis

Photosystems

Cyclic
only produces ATP
Non Cyclic (Linear)
Produces both ATP and NADPH
Photosystems I and II
Thylakoid Membrane
Photosystem II
chlorophyll a absorbs at 700 nm
Photosystem I
chlorophyll a absorbs at 680 nm

2 Stages

Stage 2
Carbon Fixation

CO2 is incorporated into an organic molecule

Calvin Cycle produces sugar from CO2 with NADPH and ATP

NADPH provides electrons to reduce CO2

ATP provides energy

Stage 1
Photophosphorylation

ATP is generated by adding a phosphate group to ADP

Solar to chemical energy

O2 is released

H2O is split for protons

Stomata

Microscopic pores
Where CO2 enters and O2 exits

Chloroplasts

cells of mesophyll
1 mesophyll contains 30-40 chloroplasts
interior tissue of the leaf

Chemical Formula

ENTIRE PROCESS
6CO2+ 18 ATP+12 NADPH +12 H2O-> C6H12O6+18 ADP +18 Pi+12 NADPH +6O2 +6H2O+ 12 H+
6CO2 +6H2O + Light Energy -> C6H12O6 +6O2
6 O2 released
6H2O extracted from soil

Cellular Respiration

Fermentation

Lactic Acid Fermentation

2 Lactate

Alcohol Fermentation

2 Pyruvate

2 Ethanol

absence of oxygen

ATP yield

TOTAL: 30 or 32 ATP
3rd stage
around 26 or 28 ATP
2nd stage
1st stage
2 ATP

Chemical Formula

C6H1206 + 6O2 -> 6 H2O + Energy
O2 becomes reduced

gains electrons

Glucose becomes oxidized

loses electrons

Outside and inside the mitochondria
Cytoplasm & Inner face of plasma membrane

Stages

Oxidative Phosphorylation
Chemiosmosis

ATP synthase

ATP synthesis

powered by the flow of H+ back across the membrane

ETC

creates H+ gradient across the membrane

NADH and FADH2 carry electrons

Proton Pumps

Transfer of electrons and release of energy at each step rather than all at once

Pyruvate Oxidation & Citric Acid Cycle
Citric Acid Cycle

2 Cycles

2 ATP 6 NADH 2 FADH2

1 Cycle

1 ATP 3 NADH 1 FADH2

8 Steps

Pyruvate Oxidation

1 Acetyl CoA per pyruvate

Glycolysis
Net

2 Pyruvate + 2H2O 2 ATP 2 NADH + 2H+

Two Phases

Energy Payoff

2 NAD+ +4 electrons +4 H+-> 2 NADH +2H+ & 2 Pyruvate + 2 H2O

4 ADP +4Pi

Energy Investment

2 ATP -> 2 ADP +2 Pi

Occurs in cytoplasm

Cell Membrane and Structure

Selective Permeability - The ability for a cell membrane to control which molecules can pass through it.
Active Transport - Membrane transport that utilizes energy to move ions against their concentration gradients.

Bulk Transport - The use of vesicles to move large molecules such as polysaccharides and proteins in bulk cross the membrane .

Endocytosis - Contents collect onto the plasma membrane, and they fuse into a transport vesicle where the contents travel within the cell.

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.

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.

Exocytosis - Transport vesicles migrate to the membrane, fuse with it, and release their contents.

Electrogenic Pump - A transport protein that helps create a voltage difference across membranes.

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)

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)

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)

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)

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.

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.

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.

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.

Plant Cells - Cell walls in plant cells help maintain water balance.

Hypotonic Solution - Solute concentration is less than that inside the cell; cell gains water. (Turgid)

Isotonic Solution - Solute concentration is the same as the inside of the cell, no net water movement. (Flaccid)

Hypertonic Solution - Solute concentration is greater than that inside the cell; cell loses water. (Plasmolyzed)

Animal Cells - Due to no cell wall, animal cells fare best in isotonic environments unless they have special adaptations.

Hypotonic Solution - Solute concentration is less than that inside the cell; cell gains water. (Lysed)

Isotonic Solution - Solute concentration is the same as the inside of the cell, no net water movement. (Normal)

Hypertonic Solution - Solute concentration is greater than that inside the cell; cell loses water. (Shriveled)

Functions of Membrane Proteins - Transport - Enzymatic Activity - Signal Transduction - Cell-Cell Recognition - Intercellular Joining - Attachment to Cytoskeleton and ECM

Structure

Fluid Mosaic Model - Describes phospholipids as a fluid component of the membrane while different types of proteins (mosaic) are present in the bilyaer.
Membrane Proteins

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.

Peripheral Proteins - Proteins that are anchored to the membrane.

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

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.

Cholesterol - Cholesterol also affects membrane fluidity. Its presence between phospholipids reduces movement at moderate temperatures and prevents phospholipids from packing tightly at low temperatures.

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.

Animal Cell Structures

Plant Cell Structures

Extracellular Components

Extracellular Matrix - Comprises of a lot of different proteins and is a network that provides structure for animal cells
Cell Wall - Provides structure for plant cell
Secondary Cell Wall - (In some cells) added between the plasma membrane and primary cell wall
Middle Lamella - Thin layer between the primary walls of adjacent cells
Primary Cell Wall - Relatively thin and flexible
Cell Junctions
Gap Junctions - Allows everthing to move between cells (Animal)
Desmosomes - Connections between cells through proteins that allow some substances to go between cells (Animal)
Tight Junctions - Membranes of adjacent cells tightly connected with proteins preventing the movement of any fluid or substance (Animal)
Plasmodesmata - Channels present between plant cells that go through cell walls, allowing the transfer of water and other nutrients (Plant)

The Cytoskeleton

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
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
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

Centrosomes - "Microtubule organizing center" that helps with cell division. (Composed of 9 sets of triplet microtubules)

Cilia - Mobility structure that occurs in large numbers on cell surface. (Cell motility, composed of microtubules (9 doublets surrounding 2 microtubules))

Flagella - Mobility structure that is limited to one or few per cell. (Cell motility, composed of microtubules (9 doublets surrounding 2 microtubules))

Intracellular Organelles

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.
Endosymbiont Theory - Origins of mitochondria and chloroplasts. Prokaryotic (non-photosynthetic and photosynthetic) cells engulfed by eukaryotic cells and formed symbiotic relationships with them. (Energy)
Chloroplast - A double membrane organelle that synthesizes food through photosynthesis

Stroma - Internal fluid

Granum - Stack of thylakoids

Thylakoid - Membranous sac

Mitochondria - A double membrane organelle that produces ATP through cellular respiration

Matrix - Space inside the inner membrane where DNA is

Intermembrane Space - Space between inner and outer membranes

Cristae - Folds within the mitochondria

Endomembrane System - Regulates protein traffic and performs metabolic functions
Plasma Membrane - To protect the cell from the surrounding environment and regulate the materials that enter and exit from the cell
Golgi Apparatus - Modifies products of the ER and moves them to their final destination

Cis Face - Receives cargo shipped out by ER

Trans Face - Releases cargo after making changes

Endoplasmic Reticulum

Smooth ER - Synthesizes lipids, metabolizes carbohydrates, detoxifies drugs and poisons, and stores calcium ions

Rough ER - Secretes glycoproteins, distributes transport vesicles, and is considered the membrane factory of the cell

Vacuoles - Large vesicles that are meant to store substances

Central Vacuoles - Found in plant cells and serves as a repository for inorganic ions and water

Contractile Vacuoles - Pump excess water out of cells

Food Vacuoles - Formed when cells engulf food or other particles

Lysosomes - Organelles packed with enzymes that promote the hydrolysis of biological molecules

Autophagy - A process that uses hydrolysis enzymes to recycle cell's own organic material

Phagocytosis - Extending a cell's membrane to engulf a foreign cell or food particle

Nucleus - Storage site for DNA
Nuclear Envelope - Double membrane enclosing the nucleus; continuous with the ER

Lamina - Protein filament meshwork that lines the inner surface of nuclear envelope and keeps its structure

Nuclear Pores - Small openings lined with porin proteins that assist in transport

Nucleolus - Site of ribosomal RNA synthesis
Chromosome - One long DNA molecule that forms when a cell is prepared to divide (CONDENSED Chromatin)

Chromatin - Material consisting of DNA and histone proteins

Ribosomes - Comprised of ribosomal RNA and protein. Produces proteins
Bound Ribosomes - Ribosomes that are on the outside of the ER
Free Ribosomes - Ribosomes suspended in the cytosol

Back to ER

Lysosomes

Membrane Protein

Secretion

Protein has different destinations

Protein gets shipped out through vesicles and then fuze onto the first phase of Golgi

Protein is now in the ER

Enzyme that cleaves the signal peptide

Signal peptidase

Protein is released in the ER lumen.

empties A site and causes everything to fall apart

Release factor

A new tRNA comes to the A site

tRNA moves to E site to be released

tRNA moves when P site is empty

amino acids added from N to C

mRNA is read from 5' --> 3'

Forms peptide bonds between amino acids

Peptidyl Transferase

Amino acid goes to the A site

tRNA carries correct amino acid

tRNA is in P site

small ribosome bind tRNA and mRNA from 5'

Termination

Elongation

Initiation

Anti-codon

Codon

tRNA

mRNA

End product is inhibitor

Pathway is halted

Locks all subunits

Binds to one active site

Affects proteins function at another site

Binds to protein at one site

inhibitor or activator

alters shape pf enzyme

binds away from active site

competes for active site

mimics substrate

Feedback

Cooperativity

Allosteric Regulation

Noncompetive

Competitive

Inhibition

Change of preffered pH

High Temperatures

Denatures by

Enzyme/Substrate

ΔG is not affected

Speeds Up Reactions

Lower activation Energy

Reactions Have

Make Coupler Reactions

System is at equillibrium

ΔG=0

Reaction can cannot occur spontaneously

Reaction can occur Spontaneously

ΔG>0

ΔG<0

Products have more free energy

Reactants have more free energy

Absorb of free enery (+#)

Realease of free energy (-#)

Exergonic

Endergonic

ΔG can be

T=Temperature (kelvin)

Δ=Change

S=Dissorder

H=Enthalpy

G=Gibbs

Equation: ΔG=ΔH-TΔS

Gibbs Free Energy

Energy trasnfer increases entropy

Energy cannot be created or destroyed

Laws Of Thermodynamics

Energy

Consume Energy

Realease Energy

Function

Multiple Structures

Multiple 3° with R-Group Interactions

3-D Shape

Alpha Helix

R-Groups Interact

Beta Pleaded Sheet

H bonds form between the polypeptides

Form Structures

Quaternary Structure

Tertiary Strucrure

Single strand of Amino acids

Secondary Structure

Primary Structure

Polypeptide

R-Group

Hydrogen

Carboxyl Group

Amine Group

Amino Acid

With sugar

Bonds phosphate group

Hydrogen atoms are across

Hydrogen atoms are on the same side

Trans

Cis

Has double bonds (kinks)

No double bonds

Liquid @room temp.

Solid @room temp.

Nucleobase

Ribose

Deoxyribose

RNA

DNA

HDL

LDL

Four Rings

Unsaturated

Saturated

Cholesterol

Phospholipids

Triglycerides

Sucrose

Fructose

Glucose

α Alpha Glucose (OH on bottom)

β Beta Glucose (OH on top)

Forms Peptide Bond

Forms Phosphodiester Bond

Forms Ester bonds

Forms Glycosidic Linkage

Macromolecules

Hydrogen, Oxygen, Nitrogen, Carbon, Phosphorus

Dehydration Synthesis
Removal of H2O

Bonds

Intramolecular (within)

Ether linkages
Membranes of Archaea (branched)
Ionic
Acidic/Basic R-groups in Tertiary and Quaternary structures of proteins
Ionic Compounds
Covalent
Double Covalent: Unsaturated Fats
Hydrocarbon chains
Ester Linkage

bond between a glycerol and fatty acid

Phosphodiester Linkage

Between the phosphate group and sugar of 2 nucleotides

Sugar phosphate backbone

Peptide Bonds

Between the amino and carboxyl group

Primary structure of protein

Nonpolar

Non-charged

Polar

Slight/ partial charges

Glycosidic Bond/Linkage

Monosaccharides to form polysaccharides

Alpha glycosidic linkages

Starch, Dextran, Glycogen, Amylose, and Amylopectin

Beta glycosidic linkages

Cellulose

Disulfide Bonds

Tertiary structure of proteins: Cysteine (R-group)

Intermolecular (between)

Dipole-ion
Between ions and polar molecules
Dipole-dipole
Strong interactions between polar molecules

Hydrogen Bonds (H to O, N, or F)

Secondary structure of proteins

forms the alpha helix and beta sheets of the one protein and occurs in the main chain only.


Water molecules

Water properties

Complementary base pairing

Hydrophobic Interactions
Phospholipid bilayer/membrane
Tertiary structure of proteins
Van Der Waals
More apparent in nonpolar molecules

BIO 311C

Topic 3: DNA Structure, Replication, Regulation, and Expression

Gene Regulation
Regulating which genes are expressed and when they are expressed

The genes are grouped in operons. Several sequences of DNA are operators that can turn on or off the gene expression.

Only at transcription level

operons (genes), operators (sequences of DNA), activators/repressors, promoters, mRNA, and proteins

Negative regulation repressors while positive regulation is associated with activators

Examples seen through the Lac Operon

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.

decreases gene expression to a basal level

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).

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.

Eukaryotes

Regulation can also occur at RNA processing, translation, and protein activity or modifications.

Transcription

Transcription Factors

General

Proximal control elements

Bring transcription levels to background or basal (meaning lower)

Specific

Distal control elements

Combinatorial control of gene expression

Liver and cell cells expressing different levels of the albumin and crystallin genes.

upstream or downstream of DNA

proximity to the gene they regulate can vary

Enhancers

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

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.

Changes level of transcription by increasing or decreasing

Activator

Repressor

DNA material present in the nucleus

DNA wraps around histones to form nucleosomes and further coil into the chromatids of chromosomes.

Translation
Transcription
Eukaryotes

RNA Splicing

Exons - Coding sequences of mRNA that are used to encode proteins.

Introns - Non-coding sequences that are removed during RNA splicing.

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.

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.

pre-mRNA Processing

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)

5' Cap - A modified guanine (G) nucleotide added to the 5' end of the pre-mRNA that will be used for translation.

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.

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)

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.

Occurs in the Nucleus (Not coupled with Translation, translation occurs in the cytoplasm.)

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.

Downstream - To the right of the transcription start site, nucleotides are numbered by positive numbers.

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.

Prokaryotes

Stages of Transcription

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.

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)

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)

Occurs in the Cytoplasm (Coupled with Translation, mRNA is made and immediately translated)

DNA Structure & Replication
DNA Replication

Replication process

Occurs in one direction

5' to 3'

Enzymes

DNA Ligase

Joins DNA together

DNA Polymerase I

Removes RNA nucleotides and replaces them with DNA nucleotides

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

Primase

Makes RNA primers at 5' end of leading strands and each Okazaki fragment

Topoisomerase

Relieves overwinding strain ahead of replication forks by rejoining DNA strands

Single Strand Binding (SSB)

Binds and stabilizes single stranded DNA and prevents it from rebinding

Helicase

Unwinds parental double helix at replication forks

Needs origin of replication (ORI)

3 Models of DNA Replication

Dispersive

Each strand of both daughter molecules contains a mixture of old and new synthesized DNA

4 helices

2 helices

Contain pieces of parental strand and pieces of new DNA

Semiconservative

Two parent strands separate and each functions as a template for a new complementary strand

2 helices

Contain one parental strand and one new strand

2 new complementary helices

Two helix

Each helix contains one parent strand and one new strand

Conservative

Two parent strands reassociate after acting as template strands and restore the parental double helix

Second Replication

One parent helix

3 daughter helices

First Replication

One new helix

One parent helix

DNA structure

Double Stranded Helix

Complementary base pairing

Purine+Pyrimidine

Guanine(G)+Cytosine(C)

Adenine(A)+Thymine(T)

Nuceotide

Bond connecting each nucleotide= phosphodiester bond

Nitrogenous base

Phosphate Group

Nitrogenous bases

Adenine (A)

Cytosine (C)

Guanine (G)

Thymine (T)

Sugar phosphate backbone

Sugar

Phosphate group

Chargaff's Rule

A+G= T+C

Guanine= Cytosine

Adenine= Thymine

3 experiments

Messleson & Stahl

Found from density bands that DNA replicates semiconservatively

Bacteria in 14N

"Light"

Bacteria in 15N

"Heavy"

Hershey & Chase

Asked what was the component that was injected by bacteriophages inside bacterial cells, DNA or Protein?

Determined DNA carried genes

Determined DNA was injected

One tube of Radioactive Sulfur (35S)

Labeled Proteins

Mixed

Centrifuged

One tube of Radioactive Phosphorus (32P)

Labeled DNA

Mixed

Shook tube to release bacteriophages from bacterial surface

Centrifuged

Recovered radioactivity inside bacterial cells

Griffith

Experiment

Heat-killed S & Living R

S. components entered live R. and changed the genetic makeup of R to S

Heat-killed S

Living R

Mouse healthy

R. strain found to be nonpathogenic

Living S

Mouse dies

S. strain found to be pathogenic

Injected mice with

R. pneumoniae

Nonpathogenic

"rough" no capsule

S. pneumoniae

Pathogenic

"smooth" presence of capsule

Topic 1: Chemical Bonds, Cell Structure and Function

Prokaryotes
Classifications

Bacteria

Archea

Extremophiles

Methanogens

Produce methane as a waste product

Swamps

Extreme Thermophiles

Extreme Temperaters

Extreme Halophiles

Highly Saline Environments

Structure

Internal Cell Structures

Periplasmic Space

Contains hydrolytic enzymes and binding proteins

nutrient processing and uptake

Ribosomes

protein synthesis

Nucleiod

contains DNA

Cell Surface Structures

Plasma membrane

Functions

Nutrient Transport

Waste Transport

Protection from environment

Permeable Barrier

Capsule & Slime layers

Adherence

Resistance

Phagocytosis

Flagella

Archaeal Flagella

Powered by ATP

Bacterial Flagella

Powered by H+ Flow

3 Main Parts

Filament

Hook

Motor

Movement

Fimbriae & Pili

Bacterial Mating

Attachment to surfaces

Cell Wall

Peptidoglycan

Gram Negative

Thin Layer of peptidoglycan

Gram Positive

Thick Layer of Peptidoglycan

Cell

Shape

Shape

Spirilla

Spiral Shape

Basillus

Rod Shape

Coccus

Spherical Shape

Topic 2: Membranes, Energy, and Cell Communication

Cellular Respiration & Photosynthesis
Metabolism
Anabolic Pathways
Catablic Pathways
Cell Signaling/ Communication
Membrane Receptors

G-protein linked receptor

Signaling molecules that use GPCR: epinephrine, hormones, and neurotransmitters

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).

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.

Transduction (amplifying): cAMP activates Protein Kinase A to transfer ATP to activate another kinases

phosphorylation cascade: kinases that phosphorylate and activate each other.

Dephosphorylation: The use of phosphates to inactivate kinases, by removing phosphate groups.

Cellular response : Will different due to the different GPCR and the cells.

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

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 ligand will unbind from receptor which then closes the ligand-gated ion 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.

Ligand (First Messenger): Hydrophilic

Location: Cell membrane

Second messenger

Location: inside the cell

Intracellular Receptors

Ligand: Hydrophobic or nonpolar molecule

Thyroid and steroid hormones

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

Physical contact

Communications through gap or plasmodesmata junctions. Physical contact communication can also occur through surface protein and binding of the surface proteins.

Local Signaling

Seen in paracrine and synaptic signaling

Long-distance signaling

Seen in hormonal signaling