Staphylo

Clustered

Cocci

Spherical

Aureus

Gold

Entero

GI tract

Coli

Colon

Bacteria

• Unicellular
• Prokaryotes
• No nucleus
• Peptidoglycan cell wall ( carb+protein)
• Binary Vision (divid into two)
• Energy= Organic compounds or photosynthesis

Viruses

• Acellular
• Core= DNA or RNA, surrounded by protein coat, may have enclosed lipid envelope
• Only replicated in living host cells

Types of Archaea

• Acidophiles - Acid loving
• Halophiles - Salt loving
• Thermophiles - Heat loving
• Alkaliphiles - Alkali loving
• Methanogens - Methan loving

What is normal microbiota and their function?

• Microbes normally present on human body
• Prevent growth of pathogens
• Produce growth factors ( vitamin k & folic acid)

Resistance factors of normal microbiota

Skin, Stomach acid, and antimicrobial chemicals

What is an emerging infectious disease (EID), what is an example.

Increasing incidences of a new disease that may have evolved or spread to a new location, Ebola.

Three types of bonds

• Ionic -Middle
• Covalent -Strongest
• Hydrogen - Weakest

Ionic bond

Attraction between ions of opposite charge. One atom loses electrons and another gains an electron.

Covalent bond

Two atoms share one or more pairs of electrons

Hydrogen Bond

• Atom that is covalently bonded to an O or N is attracted to another N or O atom in another molecule.
• Electromagnetic attraction between polar molecules

Types of chemical reactions

• Synthesis
• Decomposition
• Exchange
• Reversible

Synthesis Reaction

Atoms, ions, or molecules combine and form a new larger molecule

Glucose + Fructose = Sucrose

Synthesis Reaction

Decomposition Reaction

Molecules split into caller molecules, ions, or atoms

Sucrose = Glucose + Fructose

Decomposition Reaction

NaOH + HCI -----> NaCI = H₂O

Exchange Reaction

Exchange Reaction

Part synthesis and part decomposition

Reversible Reaction

Can go either direction

A + B ______ AB

Reversible Reaction

Acids

Substances that dissociate into one of more H⁺

HCI ---> H⁺ + CI^-

Acid

Bases

Substance that dissociate into one or more OH^-

NaOH ----> Na⁺+ OH^-

Base

What is pH

Amount of H⁺ in a solution

pH increased H⁺

Increased acidity

pH increased OH^-

Increased alkalinity

Optimum pH

7

4 organic molecules

• Carbs
• Lipids
• Proteins
• Nucleic Acids

Carbs

• Cell structure and energy source
• (CH₂O)_n
• Monosaccharides, Disaccharides, Polysaccharides

Monosaccarides

Simple sugars with 3 to 7 carbon atoms, glucose, fructose

Disaccharides

Formed when 2 monosaccarides are joined in dehydration synthesis

Polysaccharides

Tens or hundreds pf monosaccharides joined through dehydration synthesis

Lipids

• Store energy & primary components of cell membranes
• C,H, and O
• Fats, oils, waxes, phospholipids, steroids
• Non polar , insoluble in water

Saturated fat

• Saturated with the max amount of hydrogens.
• Hydrocarbon are straight and can pack close together = solid at room temp
• Cannot have anymore Hydrogens

Unsaturated fat

• Double bonds reduce the # of hydrogens
• Cant pack close together = liquid at room temp
• Small number of Hydrogens

Proteins

• Cell structure and function
• Enzymes- speed up chem reactions
• Trans. Protein- Move chem across membrane
• Flagella- made of protein
• some bacteria toxins are protein

Amino Acids

building blocks of proteins

Peptide Bonds

• Bond between amino acids
• Every peptide bond between 2 amino acids, one water molecule is released
• Formed by hydration synthesis

4 levels of protein structure

• Primary
• Secondary
• Tertiary
• Quaternary

Primary Structure

Polypeptide strand (amino acid sequence)

Unique sequence which amino acids are linked together to form a peptide chain

Genetically determined

Secondary Structure

Helix and pleated sheet (with 3 polypeptide strands)

Depends on amino acid sequence

Localized, repetitious, twisting or folding of the peptide chain.

Shape results from hydrogen bonds joining the atoms of peptide bonds at diffrent locations along polypeptide chain

Tertiary Structure

When helix folds irregularly, forming disulfide bridges, hydrogens bonds, and ionic bonds between amino acids in the chain.

Determines what protein looks like

Conjugated Proteins

• Glycoproteins
• Lipoproteins

Glycoproteins

contain oligosaccharides covalently attached to proteins

Lipoproteins

Contain both proteins and lipids, bound to the proteins, which allow fats to move through the water

Prokaryote

• One circular chromosome, not a membrane
• Bacteria: peptidoglycan cell walls
• Archaea: Pseudomurein cell walls

Eukaryote

• Paired chromosome, in nuclear membrane
• Polysaccharide cell wakks

Prokaryotic cell shapes

• Coccus- Sherical
• Bacillus- rod shaped
• Spiral
  • Spirillum
  • Vibrio
  • Spirochete

Prokaryotic Arrangements

• Pairs
• Clusters
• Chains
• Terads
• Sarcinae

Pairs

Diplococci and Diplobacilli

Clusters

Staphylococci

Chains

Streptococci and Streptobacilli

Tetrads

Divide in two planes

Sarcinae

divide in four planes

Gram Positive

• Stack of peptidoglycan
• One membrane
• Stains purple

Gram Negative

• Single layer
• Seconds membrane
• Periplasmic space

Simple Diffusion

Movement from high to low concentration

Facilitated Diffusion

Movement from hight to low concentration, but involves a transporter protein

Facilitated Diffusion: Non- Specific

Any molecule can move thought transporter protein

Facilitated Diffusion: Specific

Only certain molecules can move through transporter protein

Active Transport

Movement against concentration gradient, allows bacteria to accumulate high concentrations , needs ATP

Osmosis

Movement of water across a selectively permeable membrane, allows free movement

Isotonic

Equal on both sides, allows free movement

Hypotonic

Solution lower that osmotic pressure, less salute & more water

Hypertonic

Higher concentration of salutes inside the cell, water flows out to maintain balance.

Metabolism

Sum of chemical reactions in an organism

Catabolism

Provides energy and building blocks fro anabolism

Anabolism

Uses energy and building blocks to build large molecules

Enzymes

Facilitate and catalyze proteins

Some are highly specific based on conformation (prime,sec,&tertiary)

They are reusable

Apoenzyme

An enzyme without its cofactor, inactive

Holoenzyme

Apoenzyme plus cofactor, active

Factors that influence enzyme

• Temperature- best at 37 C
• pH- Optimum 7.2-7.4
• Substrate concentration- W/ increase the rate of increasing active site till all enzymes are at maximum
• Inhibitors - Feedback inhibition binds to molecule decreases its activity

Oxidation and reduction reactions

Both are used in catabolism to extract energy and store it in ATP

Oxidation

Removal of electrons produces energy

Reduction

Gain of electrons

Difference between resperation and fermentation

Respiration uses all 3 steps and fermentation only uses glycolysis

Three parts of respiration

Glycolysis, Krebs Cycle, and Electron transport chain

Phototrophs

Use light as primary energy source

Chemotrophs

Use energy from chemicals (oxidation reduction)

Autotrophs

use carbon dioxide as carbon source

Heterotrophs

Use organic carbon source