Water Chemistry
Properties |
1. Cohesion: water sticking to itself with hydrogen bonds (causes surface tension) |
2. Adhesion: water sticking to other polar/charged molecules (causes capillary action) |
3. High specific heat: water can absorb a lot of heat without changing temperature |
4. Excellent solvent: can bond with and 'dissolve' other charged or polar molecules |
Water is polar: it has one partially positive side (Hs) and one partially negative side (O), due to uneven sharing of electrons |
Water is polar. That polarity causes hydrogen bonds to form and makes water the solvent of life
Hydrolysis and Dehydration Synthesis
Hydrolysis |
Dehydration Synthesis |
hydro - water lysis - break down |
dehydration - remove water synthesis - building |
- process using water to break bonds in a polymer |
- process creating polymers from monomers and removing water |
Polymer + H2O -> Monomer |
Monomers -> Polymers +H2O |
Process used to build polymers (dehydration synthesis) and break down polymers (hydrolysis)
Carbohydrates
- Monosaccharides - single unit sugar (glucose, fructose, etc) |
- Polysaccharides - multiple unit sugar (starch, sucrose, lactose) |
Use for short term, quick energy |
C x
H 2x
O x
<-- chemical formula |
Carbohydrates contain CARBON, HYDROGEN, and OXYGEN
Lipids
-fatty acids, triglycerides, and phospholipids |
-stored in long chains with significantly MORE hydrogens and carbons than oxygens |
1. unsaturated fatty acids - contain a 'kink' in the tail caused by 1 or more double bonds. Liquid at room temperature due to loose packing of the fatty acid chains. Many plant fats. |
2. saturated fatty acids - very straight chain caused by full saturation of hydrogens (no double bonds). Solid at room temperature. MAny animal fats (and modified plant fats) |
Lipids contain CARBON, HYDROGEN, and OXYGEN sometimes include phosphorus
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Proteins
Primary structure: |
the sequence/order of amino acids |
Secondary structure: |
the hydrogen bonds occurring between the backbones of the amino acids (does not involve R groups) |
Tertiary structure: |
R group interactions (polar versus nonpolar, hydrophobicity, and charge) |
Quaternary structure: |
Multiple polypeptide chains |
monomer: amino acids (there are 20 total) |
polymer: polypeptide/proteins |
includes: enzymes, structural proteins, transport proteins, etc. |
Contains CARBON, HYDROGEN, OXYGEN, NITROGEN sometimes sulfur
Nucleic Acids
Nucleotides (monomer): |
contains, nitrogen base (A, T, C, G, or U), sugar (deoxyribose or ribose), and a phosphate group |
DNA |
RNA |
double-stranded |
single-stranded |
deoxyribose sugar |
ribose sugar |
genetic code found in nucelus |
genetic copy that is the intermediate to make a protein |
contains CARBON, HYDROGEN, OXYGEN, PHOSPHORUS, and NITROGEN
Enzymes
Substrate: |
reactant, acted on by the enzyme |
Active Site: |
region of the enzyme that the substrate binds to |
Enzymes are catalysts - they help speed up a reaction (lower activation energy) but are reusable |
Enzymes can be denatured - this means tht the enzyme loses it's ability to function |
- temperature changes (heat and cold), pH changes, salinity, etc. |
Enzyme and substrate concentration can also affect function |
as substrate concentration increases, the reaction rate will also increase UNTIL it reaches the saturation point |
as enzyme concentration increases, reaction rate will also increase exponentially as long as substrate presence is constant |
competitive inhibitors bind at the active site and compete with substrates |
noncompetitive inhibitors bind a different part of the enzyme and cause the enzyme to change shape and not be able to bind the substrate anymore |
Proteins that are designed to accelerate chemical reactions in living systems
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