Bio 311c group 4 final Map

Map 1

Cellular Functions and Organelles

Animal Only

Extracellular Matrix

Collagen

Fibronectin

Protoglycan

Integrins

Tight Junction

Desmosome

Gap Junction

Present in both Animal and Plant Cells

Mitochondria

Vesicles

Nucleus

Nuclear envelope

vacuoles

Endoplasmic Reticulum

Rough ER

Ribosomes

Smooth ER

Golgi Apparatus

Lysosome

Peroxisome

Cytoskeleton

Microtubules

Microfilaments

Intermediate Filaments

Plant Only

Plasmodesmata

Cell wall

Central Vacuole

Chloroplast

Prokaryotic Only

Biological Molecules

Protiens

Amino Acid

Main Chain

Amino Group

Carboxyl Group

Side Chain (R-Group)

Polar

Nonpolar

Basic

Acidic

Protien Folding

Primary

Peptide Bonds

Dehydration Synthesis

Secondary

Hydrogen Bonds

Types

Alpha Helices

Beta Pleated Sheets

Tertiary

Interaction of R-Group

Hydrogen Bonds

Ionic Bonds

Van Der Waals

Disulfide Bonds

Quaternary

Interchain Interactions

Protien Structure

Amino Acid Sequence

Physical/Chemical Conditions

pH

Temperature

Salt

Solution Prevents Disulfide Bond

Lipids

Fat Molecule

Glycerol

Fatty Acids

Unsaturated

Liquid at Room Temperature

Isomers

Trans

Cis

Double Bond

Saturated

Solid at Room Temperature

Uses Ester Linkage

Dehydration Synthesis

Phospholipids

Form Closed Liquid Bilayers

Parts

Hydrophilic Head

Hydrophobic Tails

Steroids

Cholesterol

Amphipathic

In Cell Membrane

Types

HDL

LDL

Carbohydrates

Polysaccharides

Structure

Cellulose

Linear

No Branching

Storage

Glycogen

Extensive Branching

Starch

Amylose

No Branching

Amylopectan

Some Branching

Use Glycosidic Linkage

Alpha 1, 4

Alpha 1, 6

Beta 1, 4

Bet 1, 6

Glucose

Alpha

Glycogen

Starch

Beta

Cellulose

Nucleic Acids

Types

DNA

Ribose

Thymine

Double-Stranded

Complementary Base Pairing

Uses Hydrogen Bond

RNA

Deoxyribose

Uracil

Single-Stranded

Both

Base Pairing

Use Hydrogen Bonds

Sugar-phosphate Backbone

Nucleotides

Deoxyribose Sugar

Phosphate Group

Nitrogenous Base

Cytosine

Thymine

Uracil

Adenine

Guanine

Use Phosphodiester Bond

Dehydration Synthesis

Nucleosides

Deoxyribose

Nitrogenous Base

Chemical Bonds

Intermolecular Forces

Van Der Waals

Hydrogen Bonding

Hydrophobic

Dipole-Dipole

Ion-Dipole

Intramolecular Forces

Covalent

Non Polar Covalent

Polar Covalent

Ionic

Bond Strength

Electronegativity

Water

Water Properties

Cohesion

Water Transport in Plants

Surface Tension

Adhesion

High Specific Heat

Helps moderate temperature

High Heat of Vaporization

Evaporative Cooling

Expansion Upon Freezing

Denser a Liquid than a Solid

Universal Solvent

Acids and Bases

pH

Acidic

Basic

Neutral

pOH

Molecules interacting with water

Hydrophobic

Hydrophilic

Amphipathic

Molecular Structure

Bent

Polar

Bonds

Hydrogen Bonding

Water molecules & heat

Heat is absorbed

Hydrogen bonds break

Heat is released

Hydrogen bonds form

Map 2

Cellular Respiration

Aereobic(requires Oxygen)

Glycolysis

Takes Place in Cytosol

Inputs: 1 Glucose, 2 ATP

Outputs

Net: 2 Pyruvate, 2 NADH, 2 ATP

Total: 2 Pyruvate, 2 NADH, 4 ATP

Uses Substrate level Phosphorylation to produce ATP

Step 1: Hexokinase converts Glucose to Glucose 6 Phosphate

Step 3: Phosphofructokinase converts Fructose 6 Phosphate to Fructose 1,6 Biphosphate

Pyruvate Oxidation

Inputs: 2 pyruvate, 2 CoA

Outputs: 2 Acetyl CoA , 2 NADH

Takes place in Cytosol then mitochondrial matrix

krebs cycle

Takes place in mitochondrial matrix

Inputs: 2 Acetyl CoA

Outputs: 6 NADH, 2 FADH2, 2 ATP

Uses Substrate level Phosphorylation to produce ATP

Step 1: Acetyl CoA adds its 2 Carbon groups to Oxaloacetate, forming Citrate

Step 3: Isocitrate is oxidized to alpha ketoglutarate while NAD+ is reduced to NADH

Oxidative Phosphorylation

Takes place in inter membrane space

Inputs: O2, 10 NADH, 2 FADH2

Outputs: H2O, 26-28 ATP

Uses Substrate level Phosphorylation to produce ATP

Paired Process

Electronic Transport Chain

As electrons are transferred down ETC, the energy released is used to pump H+ against concentration gradient

Chemiosmosis

H+ transported down concentration gradient using ATP Synthase (facilitated diffusion), produces lots of energy which is used for Pi+ADP=ATP

Anaerobic(doesn't require O2)

Glycolysis (info in aerobic section)

fermentation

Alchohol fermentation

inputs: 2 Pyruvate, NADH

outputs: ethanol, NAD+

Lactic Acid Fermentation

Inputs: 2 Pyruvate, NADH

Outputs: Lactate, NAD+

Takes Place in Cytosol

Glucose oxidized, Oxygen Reduced

Energy Transfer

Metabolic Pathways

Catabolic Pathways

Cellular Respiration

Anabolic Pathways

Biosynthetic Pathways

Polymerization

Photosynthesis

Thermodynamics

System

Closed System

Open Sytem

Surroundings

Laws

1 - Energy can be transferred, but not created/destroyed

2 - Energy transfer increases entropy

Energy Changes

Exergonic (ΔG0)

No Change (ΔG=0)

Energy Coupler

Powered by ATP

Transport

Mechanical

ATP Cycle

Enzymes

Catalytic Cycle

Binding of Substrate

Lowers Activation Energy

Enzyme Activity

Temperature

pH

Substrate Concentration

Function

Normal Binding

Competitive Inhibition

Noncompetitive Inhibition

Allosteric Regulation

Activators

Inhibitors

Cooperativity

Feedback Inhibition

Communication and Signaling

Cell communication

Physical Contact

Gap junctions

Plasmodesmata

Cell surface proteins

Types of signaling

Local signaling

Long distance

Cell signaling

Reception

Membrane receptors

Hydrophilic signal

G protein linked receptor

Signal binds to GPCR causing a change in GCPR shape allowing G protein to bind to it. GDP is replaced with GTP on the G protein. The activated G protein can now activate a nearby enzyme.

Ion channel receptor

Signal molecule binds to the receptor and the gate allows specific ions through a channel in the receptor

Intracellular receptors

Steroid hormone receptor

Transduction

cAMP

Binds and activates protein kinase which goes on to activates other kinases

Phosphorylation Cascade

Kinases are activated by the addition of a phosphate group

Enzymes

Kinase

Catalyze the transfer of phosphate groups from ATP to proteins

Phosphotase

Removes a phosphate group from proteins

Adenylyl Cyclase

Converts ATP to cAMP

Phosphodiesterase

Converts cAMP to AMP

Cell Membranes

Structure and Function

Phospholipid Bilayer

Hydrophilic Head

Phosphate and Glycerol

Hydrophobic Tail

Fatty Acids

Membrane Proteins

Integral (Embedded)

Peripheral (Surface Attached)

Selective Permeability

Small Nonpolar Molecules (O₂, CO₂)

Pass Freely

Large and Polar

Require Transport

Membrane Fluidity

Cholesterol

Temperature

Saturated Fatty Acids

Unsaturated Fatty Acids

Membrane Proteins and R-Groups Orientation

Hydrophilic R-Groups

Face Aqueous Exterior/Interior

Hydrophobic R-Groups

Embedded in Lipid Bilayer

Protein Structure Bonds

Primary

Peptide Bonds

Secondary

Hydrogen Bonds

α-Helices

β-Sheets

Tertiary

Disulfide Bridges

Ionic

Hydrophobic Interactions

Quaternary

Multiple Polypeptides Interacting

Map 3

Subtopic

DNA structure and replication

DNA Structure

Phosphodiester bond to link DNA and RNA monomers

Double Helix with two anti parallel strands

Nucleotide

Nitrogenous base

Phosphate group

Deoxyribose sugar (ribose sugar for RNA)r

Subtopic

Experiments demonstrating DNA is the genetic Material

Griffith’s Transformation Experiment (1928)

Setup: Streptococcus pneumoniae strains in mice -Smooth (S) strain: virulent, capsule‑producing -Rough (R) strain: non‑virulent, no capsule

Results: Live S → mice die
Live R → mice live
Heat‑killed S → mice live
Live R + heat‑killed S → mice die; live S cells recovered

Conclusion: Genes Transferable between Bacteria

Hershey-Chase Blender Experiment

Labeling: Phage protein with 35S (sulfur in protein)
Phage DNA with 32P (phosphate in DNA):

Procedure: allow phage to infect bacteria and blend

Observations after blending: 32P (DNA) found inside bacterial pellet
35S (protein) remained in the supernatant

Conclusion: DNA is what carries the genetic information not Protein

Chargaff's rule

In any double‑stranded DNA:
AA = TT and GG = CC (base‑pair stoichiometry)
Total purines (A+G) = total pyrimidines (C+T)

DNA Replication

Meselson-Stahl Experiment

Labeling: Grow E. coli in 15N (“heavy” nitrogen) then shift to 14N (“light”) medium.

Results after Centrifugation: Gen 1 → single intermediate band
Gen 2 → intermediate + light bands

Conclusion: Semiconservative Replication

3 types of replication:

Conservative: Original double helix remains intact; a wholly new duplex is synthesized.

Semiconservative: Each daughter duplex contains one parental strand and one new strand.

Dispersive: Both strands of both daughter duplexes are hybrids of old and new segments.

Parts of replication:

Origin of replication(ORI): Specific DNA region where replication begins (AT‑rich for easier strand separation)

Replication bubble: Local unwound region around ORI

Replication forks: The two Y‑shaped junctions at bubble edges where new strands grow

Enzymes for Replication

Leading-Strand Synthesis Enzymes

Helicase: unwinds the DNA duplex

Single‑strand binding proteins (SSBs): stabilize unwound strands

Primase (RNA polymerase): lays down short RNA primer

DNA polymerase III: extends primer continuously

Lagging Stand Synthesis (Okzaki Fragments)

Primase: synthesizes multiple RNA primers at intervals

DNA polymerase III: extends each primer to make Okazaki fragments

DNA polymerase I: removes RNA primers and replaces with DNA

DNA ligase: seals nicks by forming phosphodiester bonds

Bidirectional & Discontinuous Replication

Bidirectional: Two replication forks move in opposite directions from ORI.

Continuous (leading) strand: Synthesized 5′→3′ in the direction of fork movement.

Discontinuous (lagging) strand: Synthesized as short 5′→3′ Okazaki fragments away from fork; later joined.

Transcription

3 steps

Initiation

Elongation

Termination

Visual Interpretation

Start Site: +1

Upstream: -1, -2

Downstream: +2, +3

written 5' to 3'

Uracil(U) instead of Thymine(T)

Template strand 3' to 5'

Promoter Region

where RNA Polymerase and necessary transcription factors bind

Prokaryote Vs. Eukaryote

Prokaryotes

Location: Cytoplasm

RNA polymerase used

mrna, no pre-mrna

coupled w/ translation

Eukaryotes

Location: Nucleus

RNA polymerase 2

has initial pre-mrna

Poly A site, Poly A tail placed by Poly A Polymerase

5' Cap

promoter has TATA box

Transcription factors

Spliceosomes cleave introns out of Pre-mrna

Alternate splicing: Remove some introns, keep others , results in one gene expressing diverse rpteins

Gene Regulation

Prokaryotes

Operon

Promoter

Operator

Positive Regulation

Activator = On

No Activator = Off

Negative Regulation

Repressor = Off

No Repressor = On

Structural Genes

Lac Operon Example

Regulatory Sequences

Regulatory Gene

LacI

Promoter for Regulatory Gene

Promoter for Structural Genes

Operator

Lac Operon

Structural Genes

LacZ (B-galactosidase)

LacY (Permease)

LacA (Trans-acetylase)

Operator

Promoter

Options

No Lactose

Active Repressor

Operon = Off

Has Lactose

No Glucose

High Camp Level

Operon = On

Inavtive Repressor

Operon = On

Inavtive Repressor

Operon = On

Has Glucose

Low Camp Level

Operon = Off

Eukaryotes

Nucleosomes

Histone Protiens

H1

H2A

H2B

H3

H4

DNA

Histone Core

H2A

H2B

H3

H4

Steps

10-nm Fiber

DNA winds around histones

30-nm Fiber

fiber coils/folds

300-nm Fiber

forms looped domains

Metaphase Chromosome

coil further

Differential Gene Expression

Transcription Initiation

Transcription Factors

General

Basal

Specific

Activators

Repressors

Control Elements

Proximal

Sequences near promoter

Bind general transcription factors

Distal

Sequences upstream/downstream

Enhancers

bind specific transcription factors

Process

Acivator binds to enhancer

DNA bending protien brings activators to promoter

Activators bind to mediator protiens

Liver Cell vs Lens Cell Example

Lens Cell

Albumin Gene = Not Expressed

Crystallin Gene = Expressed

Liver Cell

Albumin Gene = Expressed

Crystallin Gene = Not Expressed

Translation

Accurate translation

Correct match between tRNA codon and mRNA codon

Aminoacyl-tRNA synthase

Correct match between tRNA and amino acid

Process

Initiation

Prokaryotes

Translation initiation complex

mRNA, tRNA carrying 1st amino acid, and 2 ribosomal subunits are brought together

Requires GTP

1st amino acid

Formyl-methionine

Eukaryotes

Small ribosomal subunit and tRNA first bind the 5' cap

Scans mRNA to find first start codon (AUG)

Then large ribosomal subunit comes to form translation initiation complex

1st amino acid

Methionine

Elongation

3 binding areas

P site

Holds the tRNA that carries the growing polypeptide chain

A site

Holds the tRNA that carries the next amino acid

E site

Exit site where tRNA leave the ribosome

Starts when tRNA carrying next amino acid comes to A site

Peptidyl transferase forms peptide bond between the 2 amino acids

tRNA in P site is now empty and moved to E site to be released

tRNA from A site moves to P site

New tRNA comes to A site

mRNA read in 5' to 3' direction

Amino acids added in N to C direction

Termination

Stop codon is reached in A site

Release factor sits in A site disassociating the translation initiation complex

GTP driven

Components of translation

tRNA

Single RNA strand about 80 nucleotides long

Bring correct amino acid to be added

Ribosomes

Prokaryotes

70S ribosomes

Eukaryotes

80S ribosomes

Large and small ribosomal subunit

Made of proteins and ribosomal RNA's

Codon

Set of 3 amino acids corresponding to an amino acid

Codon table

Universal

Degenerate

Noneverlapping