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45 Cards in this Set

  • Front
  • Back
Proteins
Are polymers made up of 20 different amino acids

Functions:
-Enzymes - catalyze a reaction/speed it up
-Defensive proteins (antibodies) - kill bacteria, defend your body
-Hormonal/regulatory proteins
-Receptor proteins - receive and respond to molecular signals
-Storage proteins - store amino acids
-Structural proteins
-transport proteins
-genetic regulatory proteins

-Can consist of more than one type of polypeptide chains
-Bind noncovalently with specific molecules
Carbohydrates
Sugar monomers (monosaccharides)
Nucleic Acids
4 kinds of nucleotide monomers
Lipids
fatty acids
Macromolecules
polymers with with molecule weights greater than 1,000


-may contain many different functional groups
Functional groups
direct interactions/functions

-group of atoms with specific chemical properties and consistent behavior.
-Some are polar, some are acidic, etc
Isomers
molecules with the same chemical formula but they look different
Optical Isomers
4 different atoms attached with it

- some biochemical molecules that can interact with one optical isomer are unable to "fit" the other
Biochemical Unity
macromolecules are present in the same proportions in all living organisms have similar functions
Polymer
a large molecule made up of monomers

- polymers are broken down into monomers in hydrolysis reactions
Monomer
a small molecule that forms polymers
Condensation reaction
chemical reaction in which two molecules become connected by a covalent bond and a molecule of water is released

-makes polymers
- monomers are joined by covalent bonds
Structural Isomers
molecules made up of the same kinds and numbers of atoms in which the atoms are bonded differently
Polypeptide Chains
unbranched (linear) polymers of covalent linked amino acids
Amino Acids
Have carboxyl and amino groups - function as both acid and base
-can be grouped based on side chains
- bond covalently

Exist in two isomeric forms:

D-amino acid (dextro, "right") - can be found in bacteria
L-amino acids (levi, "left") - is found in organisms
Side chains
(R-groups)
also have functional groups
Primary structure
the sequence of amino acids

- determines secondary and tertiary structure - how the protein is.
Secondary structure
a helix - right-handed coil resulting from hydrogen bonding between N-H group bonds
Tertiary
bending and folding
Denature
changing the shape of a protein
by heat: changes in pH, non polar substances
if cooled: protein goes back to original form (depends)
Quaternary structure
results from the interaction of subunits

Each subunit has its own unique tertiary structure
Proteins sometimes bind to the wrong molecules
-after denaturation
-when they are new and still unfolded
Chaperones
a protein that guards other proteins by counteracting molecular interactions that threaten their three-dimensional structure
Heat shock proteins (HSPs)
Chaperone proteins expressed in cells exposed to high or low temperatures or other forms of environmental stress
Carbohydrates
-Source of stored energy
-Transport stored energy
-Carbon skeletons for many other molecules
Monosaccharides
Simple sugars

-Have different numbers of carbons:
-Hexoses: six carbons - structural isomers
-Pentoses: five carbons

-Bind together in condensation reactions and form glycosidic linkages
Disccharides
two simple sugars linked by covalent bonds
Oligosaccharides
three to 20 monosaccharides
-May include other functional groups
-often covalently bonded to proteins and lipids
Polysaccharides
More than 20monosaccharides - starch, glycogen, cellulose
-giant polymers of monosaccharides

Starch = storage of glucose in plants
Glycogen =
Cellulose: very stable, good for structural components
Glucose
Cells use this as an energy source
-exists as a straight chain or ring form
Glycosidic Linkages
Bond between carbohydrate (sugar) molecules through an intervening oxygen atom
Carbohydrates can be...
modified by adding functional groups:

-sugar phosphate
-Amino sugars
-Chitin
Lipids
Nonpolar hydrocarboms

-van der Waals forces hold them together
-Not polymers, not covalently bonded
-Fats and oils store energy

-Phospholipids
-Carotenoids and chlorophylls
-Steroids and modified fatty acids
-Animal fat
-Nerve insulation
-oil and wax on skin, fur, and feathers repels water
Phospholipids
Structural role in cell membranes
Fats and oils
triglycerides (simple lipids)
-composed of fatty aids and glycerol
Glycerol
3 - OH groups (an alcohol)
Fatty Acid
nonpolar hydrocarbon with a polar carboxyl group
Ester Linkage
carboxyls bond with hydroxyls of glycerol
Saturated fatty acids
no double bonds between carbons

-Animal fats are usually saturated because they're packed together tightly, and they're solids at room temperature
Unsaturated fatty acids
some double bonds in carbon chain

monounsaturated:
polyunsaturated:
Amphipathic
having both hydrophilic and hydrophobic regions
Phospholipids
fatty acids bound to glycerol

--hydrophilic - the "head"

-hydrophobic - "tails" are fatty acid chains
-amphipathic
Bilayer
a structure that is two layers in thickness

-the phospholipid layer of membranes
Vitamins
Small molecules not synthesized by the body

-acquired in diet
Waxes
highly non polar and impermeable to water