Water

Small polar molecule that can hydrgoen bond.  Univsersal Solvent.  Hydolysis (broken apart).  Dehydration (formation).

Fatty Acids - buidling blocks for most complex lipids.  Can act as a local hormone for the cell

 

Triacylglyercols - 3 carbon back bone that fatty acid chains come off.  Function to store energy, and also to provide thermal insulation and padding.

 

Phospholipids -  Have a polar phosphate group.  Are amphipathic which makes them well suited as a major component of membranes

 

Steroids - 4 ringed structure.  Regulate metabolic activity

Built from a chain of amino acids linked together by peptide bonds thus proteins can be reffered to as polypeptides.  Nearly all proteins are built from the same 20 α-amino acids.  10 of these are essential

The number and sequence of the amino acids

The 3D shape formed when the peptide chain curls and folds.  Five forces create the tertiary structure:

 

1) covalent disulfide bonds between two cysteine amino acids.

2) electrostatic (ionic) interactions mostly between acidic and basic side chains

3) hydrogen bonds

4) van der Waals forces

5) hydrophobic/hydrophillic side chains pushed away/toward water

Protein loses most of its secondary, tertiary, and quaternary structure.  Once the denaturing agent is removed, the protein spontaneously refolds back to its original conformation.

Forms when 2 or more polypeptide chains bind together.  Example: hemoglobin

Have an empirical formula of C(H₂O).  Glucose is the most common form.  If there is sufficient ATP, glucose is polymerized to glycogen or converted to fat.  Plants form starch and cellulose from glucose.  Animals can digest the alpha linkages of starch and glycogen, but only bacteria break the beta linkages of cellulose (not a bacteria most animals have.

Made up of a 5 carbon sugar, nitrogenous base, and a phosphate group. They form polymers to create nucleic acids, DNA, and RNA.  Joined together by phosphodiester bonds.

Dissolved inorganic ions inside and outside the cell. They assist in the transport of substances entering and exiting the cell by creating electrochemical gradients across membranes.

Mostly globular proteins.  Acts as a catalyst by lowering the energy of activation for a reaction and increasing the rate of that reaction.  Work with substrates.  Some enzymes need cofactors to function.  Cofactors are either minerals or coenzymes (vitamins or their derivatives).

enzymes are designed to work on one specific substrate or closely related substrates.  The lock and key is where the enzyme has a specific shape (lock) that only fits a specific substrate (key).  The induced fit model is where both the enzyme and substrate are altered up binding which helps the reaction proceed.

Substrate concentration, temperature, and pH affect enzymatic reactions.

Agents that bind covalently to enzymes and disrupt their function.

Competitive Inhibitor

Compete with the substrate by binding reversibly with noncovalent bonds to the active site.  This can be undone by increasing the substrate concentration.

bind noncovalently to an enzyme at a spot other than the active site and change the conformation of the enzyme.  They cannot be overcome by adding more substrate.

modification of the enzyme configuration resulting from the binding of an activator or inhibitor at a specific binding site.  There can be negative feedback where a product downstream comes back and inhibits an upstream enzyme.  There can be positive feedback where a product comes back to activate an enzyme.

Enzymes end in -ase.  Once you know it is an enzyme, you know it contains nitrogen and that it is subject to denaturation.  Kinases phosporphyate and Phosphatases dephosphorylate

Takes place in the cytosol.  It is the first stage of anaerobic and aerobic respiration.  2 ATPs are used and 4 ATPs are produced.  In all, there is a net production of 2 ATPs, 2 Pyruvate, and 2 NADH molecules.  This formation of ATP is called substrate level phosphorylation.

Is anaerobic repsiration and includes the process of glycolysis.  recycles NADH back to NAD+.  Reduction of pyruvate to ethanol or lactic acid.

Requires oxygen.  If oxygen is present, the products of glycolysis will move into the matrix of a mitochondrion.  Once inside the matrix, pyruvate is converted into acetyl CoA in a reaction that produces NADH and CO₂

Acetyl CoA transfers 2 carbons from pyruvate to the 4 carbon oxaloacetic acid to begin the cycle.  Each turn of the cycle produces 1 ATP, 3 NADH, and 1 FADH₂.  2 Carbons are lost as CO₂ and oxaloacetic acid is reproduced to begin the cycle all over again.

A series of proteins.  Takes place in the inner membrane of the mitochondrion.  NADH is the first to be oxidized and produces from 2 to 3 ATPs.  FADH₂  produces about 2 ATPs.   The excess hydrogens on the outside of the membrane build up a gradient and then travel through ATP synthase to produce ATP in a process called oxidative phosphorylation.