Know the three monosaccharides and which one is the main nutrient in cells and monomer of polysaccharides.

- glucose - main nutrient in cells
- fructose
- galactose

Know the difference between starch and glycogen including the type of organism where they are found.  Know where glycogen is located in the body. Be able to provide examples of starches in the diet.

Starch - energy storage in plants, breaks down easily in the body.

common foods and potatoes, corn, and peas.

Glycogen - energy storage in the liver of animals, provides a fast way for body to increase glucose levels.

Cellulose or fiber: understand the importance of fiber in the diet and its importance in plants.  Know how cellulose is strucually different from starch and glycogen.

- these form strong fibers that are hydrogens bonded together.

- found in plant cell walls
- function:

   plants: structual support

   animals: important for proper digestion and waste elimination

Soluble and Insoluble fiber: Know the different functions of each of these in digestion and the foods where each is found.

Soluble fiber: these slow down digestion, these lower cholestoral.

Foods: beans, nuts, strawberries, blueberries

Insoluble fiber: these help prevent constipation, these speed up the

passage in our bodies.  Foods: whole grains and vegetables

Be able to describe the difference between saturated and unsaturated fats.

Saturated fats: no double bonds, max number of hydrogens are bonded, solid at room temperature, and it is located in animal fats.

Unsaturated fats: has 1 or more double bonds, it has kinks or bends in its tail, it is a liquid at room temperature, and it is located in plant fats.

Cis fats: these are unsaturated fats that have neen converted into solid fats by breaking the cis C = C bonds.

Trans fats: these cis C = C bonds result in trans bonds.

Problem: raise the lvels of bad fats and cholesterol, increasing heart disease.

Know the differences between monounsaturated and polyunsatureated fats.  Know the dietary sources for each of these and the health benefits that each provide.

Monounsaturated: contain one carbon = carbon double bond.  Sources: olive oil, cashews, almonds, and hazelnuts.

Benefits: lowers cholestoral and may reduce heart disease.

Polyunsaturated: contain multiple c = c double bonds.

Sources: omega-3 fatty acids -  flax-seed, fish oil, and walnuts

Benefits: lowers "bad fats" and risk of heart disease and stroke.

Steroids: know types of steroids and importance of cholesterol.

Definition: lipids linking rings of carbon's rings

Includes: steroid hormones, vitamin d, and cholesterol

Imprtance of Cholesterol: helps maintain cell membrance fluidity, precursor to steroid hormones, and tranports fats in the blood.

Be able to describe the functions of lipids.

- 1g of fat can store twice as much energy as 1g of polysaccharides

- synthesis of steroid hormones

- cushions and protects our vital organs

- helps gurad against heat loss

- fats are required for the absorption of vitamins a, d, e, and k

Phospohlipids: how is it different from fat, and what is its importance.

Difference: Phospholipids are different from fats because they contain fatty acids which are non-polar and a phosphate group which is polar.

Importance: The forms soap bubbles in solution because their non-polar tails turn inward towards the middle.  They also form membrance cells.

Know the general structure of an amino acis and what makes each amino acid unique.

General Structure:

- Alpha or central carbon

- Amine group (base)

- Carboxyl group (acid)

- R group - a variable side chain

Understand how proeteins are linked together through the formation of a peptide bond.

Peptide bond formation:

- a carboxyl group links to an amine group

- result: c-n bond

- backbone repeats the sequence n-c-c

Be able to describe the four levels of protein structure IN DETAIL!

Primary Structure: specific sequence of amino acids; determines by genes.  This determines overall proetein structure.

Secondary Structure: 

- resultes from the folding of the primary sequence of amino acids

- forms as the result of H-bonds of the polypeptide backbone

- two main types: alpha helix (spiral coil) and beta pleated sheet

Tertiary Structure:

- a 3-D structure of a polypeptide

- forms as the alpha helices and the beta pleated sheets interact with eachother

- the 3-D structure is stabilized by the interaction of the R-groups of amino acids

Quaternary Structure: Overall protein structure resulting from interactions between 2 or more polypeptide chains

Know how proteins can become denatures and the factors that affect protein structure.

Denaturation: the "melting" of a protein.

- occurs when the 3-D structure is altered

- prevents the proper functioning of the protein

- it is a reversible process

Factors:

- pH

- salt concentration

- light

- temperature

Know which level of protein structure determines overall protein structure.

the primary structure

Understand the importance of protein structure in enzyeme function.

Enzyemes are made up of proteins, so the proteins determines its structure.  The structure of the enzyeme is what allows it to bind with substrates.

R-side chains and the active site.

The R-side chains are what forms the active site.  They bond with the substrates and cause the substrate to become unstable.  It is this instability that lowers the activation energy.

Understand the the induced fit hypothesis.

Understand how temperature, pH and enzyme concntration affect enzyme function.

Temperature: the higher the temperature, the higher and faster the enzyme function.

pH: the more lower the pH, the lower and slower the enzyme function.

Enzyme Concentration: the higher the enzyme concentration, the higher and faster the enzyme function.

Understand how competitive inhibitors and feedback inhibition work.

Competitive Inhibitors: 

- inhibitors that closely resemble the enzme's substrate

- competitive inhibitors bind to the enzyme instead of the substrate, they compete for binding

- result: the enzyme catalyzed reaction rate slows down

- adding more substrate overcomes the effect of the inhibitor

Negative Feedback Inhibition:

- method used bt cells to control biochemical pathways that resut in the synthesis of molecules

- as the products increase, some of the act as a noncompetitive inhibitor and bind to a previous enzyme in the pathway

- result: the binding of the products to a previous enzyme in the pathway shuts down the synthesis of the product

- shutting down the biochemical pathway leads to a decrease in product

- as the levels of product decrease, the product stops binding to the earlier enzyme in the pathway and synthesis of the product can being again

- negative feedback inhitibion provides a continious loop of product synthesis followed by inhibition of product synthesis

List the functional groups fround in each of the following organic molecules.

Carbohydrates: hydroxyl and carbonyl

Fats: hydroxyl and carboxyl

Proteins: amino and carboxyl

Phospholipids: phophate, carboxyl, and hydroxyl

There are 20 different amino acids.  what is the key structural feature that makes each amino acid different?

the R-side chain

Understand how a dehydration and hydroylsis reaction works.

Dehydration: a reaction that forms a bond by the removal of a molecule of water

Hydroylsis: a reaction that adds water across a molecule in order to break a bond and form smaller molecules; reaction is the opposite of the dehydration synthesis reaction

Understand the three different types of isomers: stereo isomers , structural isomers and geometric isomers.

Structural Isomer: molecules with the same molecular formula with a different arragement of atoms.

Geometric Isomer: molecules with the same molecular formula with a different spatial arrangement.  This requires carbon-carbon double bonds.  There are 2 different forms cis - with Cl-Cl and H-H on the same side as eachother; trans is when Cl-H are on the same side as eachother.

Steroisomer: molecules that are mirror images of eachother.  One form is called the d-form and the other called the l-form.  This requires a carbon with 4 different groups attached.

Know the different types of functional groups found in the macromolecules.

hydroxyl, carbonyl, amino, sulfhydryl,  and phosphate.

Know the definition of a macromolecule and a polymer.

Macromolecule: large organic molecules. This includes carbohydrates, proteins, and nucleic acids.

Polymer: large molecules that are formed by joining together small, similar units called monomers. This includes carbohydrates, proteins and nucleic acids.  This is formed by dehydration reactions.