Structure & Function of Cells & Viruses

Cell Theory. o o o o
All living things are composed of cells. The cell is the basic unit of life Cells arise from only preexisting cells. Cells carry genetic information in the form of DNA

Prokaryotes o o o o o o o o
Unicellular organisms with simple cell structure. Do not contain membrane bound organelles. DNA is concentrated inside the area of the cell known as a nucleiod. Smaller rings of DNA, called plasmids replicate independently of a main chromosome. Ribosomes are small, 30S and 50S, which join to form a 70S complex. Contain a cell wall. Gram Positive Bacteria (purple stain) have a thick homogenous peptidoglycan cell wall. Gram Negative Bacteria (red/pink stain) have a much thinner peptidoglycan wall around their membrane, E. coli is gram negative.

Eukaryotes
Histones proteins associated with DNA coiling and packaging, once in complex with DNA, they form a nucleosome. Cell Cycle o
Four stages: G1, S, G2, & M

INTERPHASE

o o

G1 presynthetic gap, where cell doubles organelles, centrioles are produced. S synthetic phase, where DNA is replicated to form 92 sister chromatids, the chromosome number however remains 46.

G2 post synthetic gap, cells continue to grow and cell begins to prepare for mitosis.

MITOSIS (PMAT)

o o o o

Prophase chromosomes condense, spindle fibers develop and nuclear membrane dissolves. Metaphase chromosomes align in the center of the spindle apparatus. Anaphase sister chromatids split and are pulled to opposite poles. Telophase spindle apparatus disappears, nuclear membrane forms around each set of chromosomes, nucleoli appear, cytokinesis occurs.

Mitosis is 2N 2N o o o
Occurs in all dividing cells. Homologous chromosomes do not pair up. No crossing over.

Meiosis is 2N N o o
Occurs only in sex cells. Homologous chromosomes pair up at metaphase, forming tetrads.

Molecular Organization
Phosphatidylcholine most abundance membrane lipid. Lipids are amphipathic molecules containing a polar head group and a hydrophobic acyl chain.
Bile acids form lipids to solubilize fats during digestion, since fats are insoluble in water, theyd clump up in the duodenum making it difficult to digest them, this is why bile is secreted.

Lipids are always moving via lateral diffusion, and can also move from one lipid plane to the next by transverse diffusion (flipflop). Cis- double bonds increase lipid motility.

 Cholesterol decreases fluidity. Integral membrane proteins are embedded in the lipid bilayer, if they span the bilayer, theyre transmembrane proteins. o
Integral membrane proteins are tightly bound by hydrophobic forces.

Peripheral membrane proteins are weakly attached to the surface of the lipid bilayer, either through hydrogen bonding or
electrostatic associations.

All glycoproteins are found on the exterior of the cell membrane.

Simple diffusion is passive movement of particles down their concentration gradients, like osmosis. Facilitated diffusion substances enter and leave cells through channels down their concentration
gradients, no ATP is required.

Active Transport requires ATP hydrolysis and moves substances against their concentration
gradients.

o o

Primary Active Transport Na/K ATPase pump. Secondary Active Transport cotransport of glucose and sodium.

Organelles of the Eukaryotic Cell

Nucleus

Double membrane bound. Space between the inner and outer nuclear membrane is known as the perinuclear space. Site of DNA replication and transcription of DNA into RNA. Nuclear proteins are imported from the cytosol (after they have been made) into the nucleus through nuclear pores. DNA is highly negatively charged.

Nucleolus

This is where ribosomal synthesis (rRNA) occurs. Nucleolus is larger in cells that are activity involved in protein synthesis.

Ribosomes

Composed of RNA and protein. Eukaryotic ribosomes consist of 60S and 40S subunits to form an 80S ribosomal complex.

Smooth Endoplasmic Reticulum

 Lacks ribosomes and is involved in the synthesis of: membrane lipids, prostaglandins, and steroid hormones. SER is involved in the detoxification of drugs.

Rough Endoplasmic Reticulum

ER studded with the 60S ribosomes. Post Translational modification of proteins. Glycosylation
Golgi Apparatus

Forms small vesicles to transport proteins. Neutral pH Involved in glycosylation, sulfation, proteolysis. Cis-Face faces the nucleus. Trans-Face faces the plasma membrane.

Lysosomes

Contain hydrolytic enzymes, they are responsible for breaking down every macromolecule in the cell. If lysosomes rupture, they spill their enzymes into cytosol, and degrade and kill the cell autolysis. Contain a pH of 5. Have an ATP driven proton pump that pumps H+ into the lysosome *to maintain their low pH*.

Mitochondria

The site of aerobic respiration. Double membrane bound. Maternal DNA is mitochondrial DNA Contains their own DNA autonomous. Inner membrane contains the proteins of the electron transport chain. Mitochondrial matrix is the site of the citric acid cycle.

Proteins
Glycine a-chiral. Proline cyclic, and imino acid, helix breaker, forms kinks. Tryptophan, phenylalanine, tyrosine aromatic. Cysteine disulfide bonds (only a.a. that forms covalent) BASIC AMINO ACIDS histidine, Arginine, lysine (HAL) ACIDIC AMINO ACIDS Aspartic acid, Glutamic acid.

Secondary Structure

Alpha-helix forms very readily because it makes optimal use of hydrogen bonding between CO and NH groups. o o o
1.6 angstroms between residues. 3.6 amino acids per turn. Alanine loves alpha helices, bulky groups (like aromatics) hinder helix formation.

Beta-strands tend to form barrels with hydrophobes in the core.

Tertiary Structures

Covalent Disulfide bonding Ionic interactions b/w acidic and basic residues Hydrogen bonding Van der waals interactions Hydrophobic interactions

Glycoproteins are always on their way out or are extracellular membrane bound.

DENATURING AGENTS Urea Salt or pH Mercaptoethanol Organic solvents Heat

DISRUPTED FORCES Hydrogen Bonds Electrostatic (ionic) interactions Disulfide Bonds Hydrophobic Interactions Everything

Enzymes
Enzymes lower the Ea of both, forwards and backwards reactions. Increases rate of forward and backwards reactions. Does not affect G. Many enzymes require the incorporation of a non-protein molecule to become catalytically active. They are called cofactors, and
can aid in substrate binding, OR the stabilization of the active conformation.

Apoenzyme an enzyme that requires a cofactor but doesnt have it yet. Holoenzyme an enzyme with its cofactor. Cofactors bind enzymes with either strong (prosthetic groups) or weak covalent bonds. Two important cofactors include: Zn2+ and Fe2+, these are called coenzymes. Coenzymes cant be synthesized by the body, they must come from diet. At high substrate concentrations, reaction rate approaches Vmax. Optimal enzyme activity for most enzymes occurs at pH 7.2.

Enzyme Regulation is accomplished in many ways, notably through allosteric and inhibitory. Allosteric Inhibitors stabilize the inactive form of an enzyme. Allosteric Activators stabilize the active form promoting catalysis. Competitive Inhibitors bind to the active site, competing for it. Non-competitive inhibitors bind to a site other than the active site. Irreversible inhibitors permanently destroys enzyme.