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72 Cards in this Set

  • Front
  • Back
macromolecule
large organic polymer
polymer vs monomer
a polymer is a large molecule consisting of similar or identical subunits (monomers)
polymerization rxn/ dehydration rxn
builds polymers, requires energy and enzymes
hydrolysis
breaks polymers down by adding water, releases energy but also requires it
monosaccharides
carbs: simple sugars monomers
Fxn: components of structural carbs or provides energy and nutrition to cells
Ex: glucose, fructose, galactose
Disaccharides
2 monosaccharide slinked via dehydration synthesis and held by a glucosidic linkage (covalent bond)
Ex: glucose + glucose= maltose
glucose + Galactose= lactose
Glucose + fructose= sucrose
Glucosidic linkage
covalent bond in disaccharide
energy storage polysaccharides
starch (plants--> glucose stored in leukoplasts)
Glycogen (animals--> stored in muscles and liver)
structural polysaccharides
cellulose
- plants
- polymers of glucose= insoluble fiber
-symbiotic microbes digest cellulose
Chitin
-exoskeletons and cell walls in arthropods and fungi
-tough and leathery
-mineralizes with CaCO3
-used in sitiches
Lipids
non polar, hydrophobic
4 classes of lipids
waxes, fats/oils, phospholipids, steriods
waxes
used for waterproofing
structure of fats
1. gylcerol (3 carbon alcohol)
2. 3 fatty acids (hydrocarbon chains with carboxyl)
3. ester linkage (btwn, carboxyl of fatty acid and hydroxyl of glycerol)
Saturated Fats
solid at room temp., only single bonds between carbons
saturated with respect to hydrogen

made by animals
unsaturated fats
liquid at room temperature,at least one double bond within hydrocarbon chain (forms kinks in chain)
not saturated with respect to hydrogen

made by plants, seeds, and fish
Trans fats
produced by hydrogenation

Decrease HDL
- lots of protein, less cholesterol 'good'

Increase LDL
-lots of cholesterol less protein 'bad'
Function of Lipids
1. energy storage
2. cushioning/protection
3. insulation (subcutaneous fat protects from change in temp)
Phospholipid structure
glycerol, 2 fatty acids, phosphate group
Phospholipid fxn
'dual nature' ambivalent behavior in water
hydrophilic head
hydrrophobic tail

make up cell membranes in phospholipid bilayers
micelles
phospholipid rings spontaneously formed
Steriod Structure
4 fused carbon rings with varied attachments
Steriod fxn
cholesterold (component of cell membranes)
steriod hormones (testosterone and estradiol)
Nucleic Acid Fxn
1. regulate all cell functions
2. hereditary material
3. instructions for protein synthesis
Nucleic Acid Structure Monomers
monomer: nucleotides
1. phospate
2. pentose
DNA deoxyribose
RNA ribose
3. nitrogenous base
Purines
2 interlocked rings

Adenine and Guanine
pyrimidines
one single ring

cytosine
thymine, uracil (only DNA)
Nucleic Acid Structure Polymers
RNA single stranded
DNA double helix held together by hydrogen bonds
phosphodiester bonds
link sugar to phosphate in nucleic acid polymers
Protein Fxn
diversity functions depends on conformation
Protein monomer
amino acid
Structure of an amino acid
amino group, carboxyl group, hydrogen, side chain 'R' group
"R" group
warible group, 20 different amino acids with different "R" groups
three possible inoic states of an amino acid
1. NH3+ & COOH
2. NH3+ & COO-
3. NH2 & COO-
polymerization
polymer becomes a polypeptide via protein synthesis
peptide bonds
link amino to carboxyl between amino acids
"native conformation"
shape of protein under normal biological conditions, spontaneous folding
denaturation
loss of native conformation caused by temperature change, change in pH, organic solvents (nonpolar)
Primary structure
amino acid sequence determined by DNA
Secondary Structure
hydrogen bonds between amino and carboxyl groups on different amino acids

does not involve side chains

e. alpha helix and beta pleated sheet
Tertiary structure
interations between side chains
ex. hydrogen bonds and hydrophobbic interactions and inco/covalent bonds and disulfide bridges
disulfide bridges
interactions between sulfhydryl groups
Quaternary Structure
multipple polypeptide fold together
determining factors in protein conformation
physical and chemical env. in addition to primary structure
metabolism
totality of an organisms chemical rxns
catabolic pathway
exergonic, break things down
exergonic
release energy
anabolic pathway
endergonic, build things
endergonic
absorb energy
energy coupling
linking a catabolic/energy yielding process to an anabolic/energy absorbing process
1st law of thermodynamics
conservation of energy
2nd law of thermodynamics
entropy (disorder) inceases in nature
ATP
adenosine triphosphate
ATP--> ADP+ a phosphate group+energy!

3 phospates held together by high energy bonds which release energy when broken

nucleotide
catalysts
accelerate rxnz without being changed

enxymes are organic catalysts
activation energy
amount of energy reactant molecules must absorb to start rxn
enzymes
1. proteins
2. lower activeation energy so rxns are possible under cellular conditions
3. do not change nature of rxns, can be reused
4. very selective for which rxn they catalyze
substrate
substance enzyme acts upon
active site
region of enzyme that binds to substrate
induced fit
change in shape of active site in response to the substrate itself
enzymatic cycle
E+S--> ES--> P+E (product and unchanged enzyme)
enzyme substrate complex
enzyme can act on approx. 1000 substrate molecules per second
effect of pH on enzyme activity
change in pH causes denaturaiton

low pH causes enzyme to gain H+ and high caused enzyme to lose them therefore changing shape
effect of temperature on enzyme activity
increased temp yields increased substrate enzyme collions--> increased rxn rate
BUT beyond optimal temp.:
vibratory movements from increased KE disrupt bonds required for 3D structure of enxyme
cofactors
small non protein factors required for proper enzyme fxn
coenzymes
organic vitamins
minerals
inorganic cofactors
competitive inhibition
inhibitor bind to/block the active site
noncompetitive inhibition
inhibitor does not enter active site rather binds away from active site but changes the shape of the enzyme
Allosteric Regulation
binding at one site causes change elsewhere
conformational change in one subunit affects all other subunits

typically in a mulitsubunit enzyme allosteric sites exist where subunits join
allosteric activator
stabilizes active form of enzyme
allosteric inhibitor
stabilizes inactive form of enzyme
feedback inhibition
the product of a metabolic pathway truning off its own production by inhibiting a step in the pathway
enzyme cooperativity
a substrate molecule primes an enzyme to accept additional substrate molecules more readily