Chapter 2 Flashcards
Organic
containing carbon
Inorganic
doesn’t contain carbon
Waters useful physical properties?
- cohesive behavior
- temperature moderating properties
a. high heat capacity
b. high heat of vaporization - Water is a good polar solvent
Cohesive Behavior
water molecules easily hydrogen bond to one another
- water molecules are polar (one positive and negative end)
- 2 water molecules stick together by attaching a positive to a negative end forming a hydrogen bond
Temperature moderating properties
a. High heat capacity
water strongly resists increases in temperature
-when you apply heat to water, it takes longer to heat up because the hydrogen bonds have to break first in order to get the water molecules to move faster
Temperature moderating properties
b. High heat vaporization
water absorbs a lot of heat before evaporating
-evaporative cooling- sweating
Water is a good polar solvent;
water is good at dissolving solutes that are charged
- water molecules cant dissolve nonpolar solutes (nonpolar doesn’t have a charge)
- water molecules stick to the surface = dissolved
Salts
ionic substances that do not have hydrogen (H+) as a cation or hydroxide (OH-) as a anion
ex: NaCl (Na+, Cl-)
- salts act as tissue- hardening agents (e.g. in bone)
- salt solutions are electrolytic (conducts electricity)
Acids
substances that release hydrogen (H+) ions when dissolved
ex: HCL = H+ CL
- the greater [H+] (the concentration of hydrogen) the more acidic
Bases
substances that accept hydrogen (H+) ions from solution
-the lower the concentration of H+ the more basic
pH scale
logarithmic scale from 0 to 14 -pH 7 = neutral -pH greater than 7 = given to the bases -pH less than 7 = give to acids -if the pH decreases by a whole number the solution is 10x more acidic ex: 5 is 10x more acidic than 6 4 is 100x more acidic than 6
4 kinds of organic compounds found in living things?
- carbohydrates
- lipids
- proteins
- nucleic acids (DNA, RNA)
Dehydration synthesis
monomers are combined into a polymer with the removal of water
ex: [ ]-OH H-[ ] ( [ ] = monomer)
l
( H come together )
l
H H
\ / = [ ]–[ ] (polymer)
(H20) O
Hydrolysis
a polymer is broken into monomers with the addition of water
Carbohydrates
contain carbon, hydrogen, oxygen (C,H,O) in an approximate 1:2:1 ratio ex: C5 H10 O5 C6 H12 O6 -preferred fuel at cellular level( cells will always take carbs) -easily converted into fats -three categories: monosaccharides- one sugar disaccharides- two sugars polysaccharides- many sugars
Monosaccharides
carbohydrate monomer (simplest carbohydrate)
- rings of 5-6 carbons with lots of H and O
- cells can only take in carbs in this form
ex: glucose, fructose
Disaccharide
two monosaccharides that have been joined via dehydration synthesis
ex: lactose (dairy), Sucrose (table sugar), Maltose (grains)
Polysaccharides
many sugars
-two kinds/two uses:
1. some are easily broken down and are used for energy storage
ex: starch (plants), glycogen (animals; muscles (human),
liver)
2. some are difficult to break down and are used for protection
ex: cellulose (plant cell walls)
Lipids
usually nonpolar (no electrical charge) and insoluble in water (don't dissolve well) (hydrophobic) -3 kinds Triglycerides Phospholipids Steroids
Triglycerides
“fat molecules”
function- energy storage- preformed means of storing calories
-fat stores at least twice the calories of other nutrients
-contains 3 fatty acids (chains) and glycerol (the 3 C sugar)
Phospholipids
contains- phosphate containing group, glycerol, 2 fatty acids (chains)
-its amphipathic- having both polar and nonpolar regions
-found in membranes
polar “head” nonpolar “tails”
Steroids
- have many functions
ex: some act as vitamins (A,D,E,K) - some act as hormones (estrogen, testosterone)
- some are anti-inflammatory agents (hydrocortisone)
- honeycomb backbone
Proteins
polymers made from monomers called amino acids -every 20 amino acids have an amino group and a carboxylic acid group
Dipeptide
take 2 amino acids and attach them to one another
Sequence of less than 50 amino acids?
polypeptide
Sequence of 50 or more amino acids?
potein
What determines the function of a protein?
Its shape
A proteins shape is determined by what?
amino acid sequence
Amino acid sequence =
proteins primary sequence
Localized binding/ folding of amino acid chain =
its secondary structure (know one part of what the structure looks like)
Tertiary structure
a proteins overall 3-D shape
Quaternary structure
several tertiary structures working as a unit
Fibrous Proteins
long thread-like appearance
- elongate, huge
- sturdy
- building materials (use + repair yourself)
Globular proteins
- intricate (complex) shapes
- fragile
- use their shapes to interact (or grab) with other chemicals
ex: eznymes
Enzyme
globular proteins that act as catalysts (help reactions occur more quickly and efficiently
- an enzyme uses its ACTIVE SITE to adhere to SUBSRATES and then places the substrate in the correct position for a reaction to occur
- reuseable
Nucleic acids
monomers build from polymers called nucleotides
Nucleotide structure
3 parts
- phosphate group
- pentose (5 carbon sugar)
- nucleotide base (A,G,C,T)
RNA
ribonucleic acid
- single stranded
- uses A,G,C,U (not T)
- uses the pentose Ribose
- RNA molecules build proteins out of amino acids
DNA
deoxyribonucleic acid
- double stranded
- uses A,C,G,T (not U)
- uses the pentose Deoxyribose
- DNA is the instructions for making proteins
Adenosine Triphosphate (ATP)
provides energy to chemical reactions
