AP Bio: Organic Chem review (chaps. 4, 5, 8) Flashcards

Terms Definitions
compounds that have the same no. of atoms of the same elements, but different structures & hence different properties
structural isomers
isomers that differ in the covalent arrangements of their atoms
geometric isomers
isomers that have the same covalent partnerships, but different spatial arrangements
isomers that are "mirror images" of each other
functional group
a specific configuration of atoms commonly attached to the carbon skeletons of organic molecules and usually involved in chemical reactions
long molecule consisting of many similar or identical building blocks linked by covalent bonds
repeating unit that serves as the building block of a polymer
ribose, ribulose
Name two 5-carbon sugars.
glucose, galactose, fructose
Name three 6-carbon sugars.
common suffix of sugars
What is the major function of monosaccharides?
glycosidic linkage
a covalent bond formed between two monosaccharides by a dehydration reaction
disaccharides and polysaccharides
Where are glycosidic linkages found?
What is the most common disaccharide made by plants?
What is the most common disaccharide made by mammals? (Hint: What do mammals feed their babies?)
glucose, glycosidic linkages
Starch, cellulose, and glycogen are all polymers of _____ molecules joined by _____ _______.
plant cell walls
What is composed of cellulose?
plants, energy
Starch is stored by ____ to store ____.
glycogen, energy
_____ is stored by animals to store _____.
arthropod exoskeletons and fungi cell walls
What are two things composed of chitin?
They mix poorly with water.
the main characteristic of all lipids
hydrocarbon regions
Lipids are made primarily of _____.
fats, phospholipids, steroids
What are the 3 main types of lipids?
double bond; unsaturated
What causes the "kink" in a certain kind of fatty acid, and what kind of fatty acid is that (saturated or unsaturated)?
Do saturated or unsaturated fatty acids solidify at room temp.?
Are saturated or unsaturated fatty acids unable to solidify at room temp.?
energy storage, cushioning for vital organs, insulation
List 3 functions of fat.
Which is richer in energy: fats, or polysaccharides?
cell membranes
What do phospholipids make up?
They assemble into rings when placed in water; hydrophilic heads facing outwards, hydrophobic tails facing inwards. These rings form protective cell membranes.
How does the two-ended structure of a phospholipid affects its function? (THEME QUESTION!!!)
common component of animal cell membranes, other steroids are made from it
What are two functions of cholesterol?
chemical messengers that control bodily processes
What is the function of hormones?
branch of chemistry that studies carbon compounds
What is organic chemistry?
a "life force" governs processes of living things instead of the chemistry of nonliving matter
the chemistry of living things is the same as the chemistry of nonliving things
peptide bond
the bond linking two amino acids
dehydration reaction
What reaction forms a peptide bond?
primary structure
level of protein structure defined by the protein's unique sequence of amino acids
secondary structure
level of protein structure defined by the coils and folds of polypeptide chains
tertiary structure
level of protein structure defined by the overall three-dimensional shape of a polypeptide
quaternary structure
level of protein structure defined by the overall three-dimensional shape of the protein
alpha helix
coil held together by hydrogen bonding between every fourth amino acid; defines secondary protein structure
beta pleated sheet
folds formed by two or more regions on a polypeptide chain bonding to parts of a parallel polypeptide chain via hydrogen bonds; defines secondary protein structure
alpha helix, beta pleated sheet
What two main structures are involved in secondary protein structure?
hydrophobic interaction, ionic bonds, hydrogen bonds, disulfide bridges
What four main interactions are involved in tertiary protein structure?
hydrophobic interaction
water molecules exclude nonpolar molecules as they form hydrogen bonds with hydrophilic ones, thereby pushing hydrophobic side chains to the protein core; defines tertiary protein structure
ionic bonds
bonds between charged side groups; defines tertiary protein structure
hydrogen bonds
bonds between polar side chains; defines tertiary protein structure
disulfide bridges
amino acids with sulfhydryl groups are close together, causing sulfur atoms to form covalent bonds with each other; defines tertiary protein structure
protein that assists in the proper folding of other proteins
process wherein a protein unravels and loses its native shape
altered pH, salt concentration, temperature
List three things that can cause denaturation.
secondary, tertiary, quaternary
What levels of protein structure are affected by denaturation?
the totality of an organism's chemical reactions
catabolic pathway
releases energy by breaking down complex molecules into simpler ones
anabolic pathway
consumes energy by building complex molecules from simpler ones
What pathway is this an example of? : Glucose and other stuff is broken down into carbon dioxide and water (cellular respiration)
What pathway is this an example of? : Proteins are built from amino acids (protein synthesis)
second law of thermodynamics
What is this? : "Every energy transfer/transformation increases the entropy of the universe."
quantity that defines a system's disorder or randomness
less than zero
In order for a reaction to occur spontaneously, its free energy (ΔG) should be ____ ____ _____.
free energy
energy that can perform work when temp. & pressure are uniform throughout the system
exergonic reaction
reaction that has a net release of free energy (ΔG is negative); spontaneous
endergonic reaction
reaction that absorbs, or has a net gain of, free energy (ΔG is positive); nonspontaneous
energy coupling
the use of an exergonic process to drive an endergonic one
The hydrolysis of ATP produces ____ kcal/mol
a macromolecule that acts as a catalyst
activation energy
energy required to contort reactant molecules so that the bonds can break
nonprotein "helper" for catalytic activity
a cofactor that is also an organic molecule
competitive inhibitor
molecules that resemble substrates but lock into active sites to prevent proteins from working; "competes" with a substrate
noncompetitive inhibitor
molecules that bind to another part of the protein, thereby messing up the active site shape and making it function less efficiently
allosteric enzyme
an enzyme whose function at one site is affected by the binding of a regulatory molecule at another
allosteric site
active sites on allosteric enzymes
cooperative binding
binding of one substrate molecule to the active site of one subunit; locks all others into "active form"
feedback inhibition
process wherein a metabolic pathway is switched off by the inhibitory binding of the pathway's end product to an enzyme that acts early in the pathway
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