1. pH
1.1. Buffers
1.1.1. a solution where when a weak acid of base is added the net pH is not changed. the ions are able to form and reform to balance pH i.e.: Carbonic acid will form Bicarbonate and H+ ions and vice versa to balance the pH: crucial for homeostasis
1.2. Acid
1.2.1. A solution that has less concentration of Hydroxide(OH-) Ions than hydronium Ions(H+)
1.3. Base
1.3.1. A solution that has a higher concentration of Hydroxide(OH-) Ions than hydronium Ions(H+)
1.4. pH is measure in powers of ten and on a integer scale from 1-14, 1 being acidic and 14 being basic. 7 is neutral.
2. Hydrogen Bonds-
2.1. Electronegativity
2.1.1. the tendency for an atom of a given chemical element to attract shared electrons when forming a chemical bond
2.2. when O or F is present due two there high electronegativity they are able to form strong, temporary, forces or "bonds" between 2 or more molecules.
3. Properties of Water
3.1. Cohesion
3.1.1. waters ability to stick to itself
3.2. Adhesion
3.2.1. waters ability to stick to other surfaces
3.3. Density
3.3.1. water is more dense at its liquid state than its solid state which is because when water freezes in a crystaline structure which is less dense than when water is at its liquid states.
3.3.1.1. This allows for life to be viable in body of water that freeze.
3.4. Surface Tension
3.4.1. Due to waters ability to make hyrdogrn bonds and its cohesive nature. the surface of water can be interacted with, without being broken allowing for small bugs to stride across. refer to penny and dropper lab.
3.5. Specific Heat
3.5.1. Because water makes hydrogen bonds it SH is higher because it take a lot of energy to break those bonds and change the temperature of water
3.6. Solvent
3.6.1. water is a polar molecule and is able to make hydrogen bonds and break ionic bonds making it very suitable to dissolve most substances in. Exception would be nonpolar molecules.
4. Ionic Bonds
4.1. The taking and giving of electrons amongst atoms. Creates ions in the process that are attracted to each other.
5. Covalent Bonds
5.1. Polar- the unequal sharing of electrons amongst the atoms in the molecule. Will dissolve in water and disassociate ions readily most of the time. (water, sugars, nucleic acids, etc...)
5.2. Nonpolar- All of the electrons in the molecule are even distributed creating no slightly - or + regions. Do not dissolve readily in water or other polar substances. Hydrophobic. (lipids, methane, etc...)
6. Macromolecules
6.1. Carbohydrates
6.1.1. Monomer: Monosaccarides
6.1.2. Function: structure (cellulose and chitin or energy storage (starch and glycogen)
6.1.3. Structure: ringed Carbon Oxygen and Hydrogen
6.2. Lipids
6.2.1. Monomer: N/A
6.2.2. Function: long term energy storage, steroids, cell membrane
6.2.3. Structure: a glycerol back bone with glycerides attached with ester bonds.
6.2.3.1. Saturated: all of the carbons have single bonds and are filled with hydrogen. Solid at room temp
6.2.3.2. Unstaurated: 1+ of the carbons has a C=C double bond therefore causing a kink in the glyceride. liquid at room temp
6.3. Nucleic Acids
6.3.1. Monomer: nucleotides
6.3.1.1. Phosphate and ribose(suagar) Backbone with a varying nitrogenous base (ATCG or U)
6.3.2. Function: provides instruction for cell function and transport within the cell(tRNA)
6.4. Proteins
6.4.1. Monomer: Amino Acids
6.4.1.1. Structure: Central Carbon bonded to an Amino group(NH2) a Carboxyl Group(COOH), a alpha hydrogen and an R-Group
6.4.1.1.1. R-Groups- determine the overall properties of the amino acids. Affect the interaction that happen between amino acids. Can be hydrophobic(nonpolar), Hydrohpillic(polar), negativley charged, and positivley charged.
6.4.2. Function: They do most of the work in cells and are required for the structure, function, and regulation of the body's tissues and organs.
6.4.3. Structure: made up of different levels
6.4.3.1. Primary: the sequence of amino acids
6.4.3.2. Seconday: the alpha helixes or beta sheets that form within the polypeptide
6.4.3.3. Tertiary: the overall 3-d shape of the polypeptide
6.4.3.4. Quaternary: the shape formed when multiple polypeptides interact to for a protein
6.5. Dehydration Synthesis
6.5.1. water is removed from 2 molecules to form a covalent bond
6.6. Hydrolysis
6.6.1. water is added to break apart a polymer into its monomers.