Chapter 2: Inorganic and Organic Chemistry Flashcards
ion
a charged atom
ionization
the formation of ions by loss of electrons
Lewis Dot notation
a form of electron notation that involves only drawing the valence electrons
isotope
an atom that has a different number of neutrons than other atoms with the same atomic number
radioisotopes
radioactive isotopes
atomic mass
the number of neutrons plus the number of protons
Van Der Waal’s interactions
weak interactions between regions of nonpolar molecules, resulting from charge fluctuations within molecules
electronegativity
the measure of an atom’s tendency to hold or gain electrons
electrostatics
describes the tendency for positive and negative charges to attract
ionic bonds
form from the attraction of the oppositely charged ions
covalent bonds
form when the differences between the electronegativities of atoms are equal or similar
polar covalent bonds
result when one atom in a covalent bond is more electronegative than the other
hydrogen bonds
form from interactions between a partially positive hydrogen in one molecule and a partially negative atom (usually oxygen or nitrogen) in another molecule
solvent
a fluid in which molecules dissolve
dissociation
the breaking apart of molecules
specific heat
the amount of heat needed to raise the temperature of one gram by one degree Celsius
solubility
a substance’s ability to dissolve other substances
hydration shells
the result of separating ions from each other in a water molecule
adhesion
the property of water to cling to other materials because of its ability to form hydrogen-bonds
cohesion
the property of water to cling to other water molecules because of its ability to form hydrogen-bonds
surface tension
the result of cohesion, where a net force that acts on water molecules on the surface forms a “film” of tightly packed molecules
turnover
the process of water on the surface sinking as it approaches 4 degrees Celsius, and drawing up warmer water from the bottom
hydrophobic
water fearing
hydrophilic
water loving
detergent
a molecule that is polar on one end and nonpolar on the other, and can thus interact with nonpolar and polar substances to mix the two.
acid
a proton donor
base
a proton acceptor
buffer
a substance that helps to maintain a constant pH
organic chemistry
the chemistry of carbon-containing molecules
structural isomers or constitutional isomers
molecules that have the same formula, but whose atoms are arranged differently
geometric isomers
molecules that have the same formula, but have atoms arranged differently about a double bond
Enantiomers
isomers that are mirror images of each other and are not superimposable
functional side groups
parts of organic molecules that have their own characteristic properties
the hydroxyl group
consists of an —OH
carbonyl group
consists of an oxygen atom double-bonded to a carbon atom (CO)
carboxyl group
consists of a carbon with a double-bonded oxygen atom and a hydroxyl group (COOH)
amine group
consists of an —NH2 group
carbohydrates
macromolecules that play a role in energy storage and structure
monosaccharides
simple one-sugar molecules that consist of carbon, hydrogen, and oxygen
trioses
three-carbon monosaccharides
pentoses
five-carbon monosaccharides
hexoses
six-carbon monosaccharides
dehydration synthesis
the process by which two monosaccharides are linked together to form a disaccharide
hydrolysis
the process by which a disaccharide is separated into two monosaccharides
monomer
a subunit of a polymer
glycosidic linkage
the bond between monosaccharides
lipids
molecules that are nonpolar and insoluble in water
fatty acid
a carboxylic acid consisting of a hydrocarbon chain and a terminal carboxyl group
ester linkage
the linkage between a fatty acid and glycerol molecule in a triglyceride
respiration
the process by which the energy stored in triglyceride bonds in released
saturated fatty acid
a fatty acid that has as many hydrogen atoms as possible on the carbon chain
unsaturated fatty acid
a fatty acid that has double bonds within the carbon chain, and therefore fewer hydrogen atoms
phospholipid
a type of lipid that has a hydrophilic, polar head, and hydrophobic, nonpolar tails
steroids
lipids that consist of four fused carbon rings
waxes
lipids that make up leaf cuticles and organ protective filters
nucleotides
the subunits of polymers
purines
two-ringed molecules that include adenine and guanine
pyrimidines
one-ringed molecules that include cytosine, thymine, and uracil
deoxyribose
the pentose sugar that makes up the nucleotides of DNA
ribose
the pentose sugar that makes up the nucleotides of RNA
what is the central dogma of biology?
DNA makes RNA, which makes proteins
conformation
the specific shape of a protein, as determined by its primary structure
R group
a group in which a carbon or hydrogen atom is attached to the rest of the molecule
peptide bond
a bond between amino acids, which is formed by dehyration synthesis
polypeptide
a chain of amino acids bonded together, with an amine group on one end and a carboxyl group on the other
what are the charged amino acids?
AGLAH: aspartic acid, glutamic acid, lysine, arginine, histidine
what are the polar amino acids?
CATTGS: cysteine, asparagine, tyrosine, threonine, glutamine, serine
what are the nonpolar amino acids?
PALM PIG TV: phenylalanine, alanine, methionine, proline, isoleucine, glycine, tryptophan, valine
primary structure
the specific sequence of amino acids in a polypeptide
secondary structure
the regular pattern of local hydrogen bonding within the polypeptide chain
tertiary structure
three-dimensional folding that results from interactions between R groups
hydrophobic interactions
tertiary structure interactions that occur when amino acids with hydrophobic (nonpolar) R groups fold into the center of the polypeptide because water repels them
Van der Waals interactions (between R groups)
in the tertiary structure of a protein, these weak interactions occur between hydrophobic (nonpolar) R groups as they fold into into the center of the polypeptide
ionic bonding (between R groups)
tertiary structure interactions that occur between R groups of opposite charges
disulfide bridges
teritary structure interactions that result in strong covalent bonds that form between two sulfhydril groups of cysteine
quaternary structure
the final structure of a protein that results from interactions between polypeptides
mutation
a change in DNA, which results in different RNA, which could result in a different sequence of amino acids, and possibly a non-functioning protein
the first law of thermodynamics
energy can neither be created nor destroyed
the second law of thermodynamics
every energy transfer results in an increase in entropy
entropy
the measure of randomness or disorder in a system
exergonic reaction
a reaction that has a negative amount of free energy, and thus gives off energy
catabolism
all of the metabolic processes that give off energy, and involves the breakdown of molecules
anabolism
all of the metabolic processes that require an input of energy. These reactions typically involve the synthesis of new molecules.
energy coupling
the process by which energy released from an exergonic reaction is used to feul an endergonic one
activation energy
the energy required to start the reaction
enzymes
proteins that serve as catalysts of biological reactions
endergonic reaction
a reaction that has a positive amount of free energy, and thus requires energy to be put into it to function
induced-fit model
the hypothesis for enzyme action, where the substrate induces a more complete fit of the enzyme’s active site around it
competitive inhibitor
an inhibitor that competes with the substrate for the active site
noncompetitive inhibitor
an inhibitor than can bind to a part of the enzyme other than the active site permanently, ceasing that enzyme’s function
catalytic cycle
the enzyme mechanism in which the substrate fits into the active site, the bond is broken, the products are released, and the enzyme remains intact
allosteric regulation
a type of enzyme regulation that uses molecules to inhibit or activate the enzyme by binding to a place other than the active site (called the allosteric site)
allosteric activator
an activator that binds to the enzyme and keeps it in an active state, where the active site is exposed
allosteric inhibitor
an inhibitor that binds to the enzyme and keeps it in an inative state, where the active site is inaccessable
feedback inhibition
a type of enzyme regulation that involves the inhibition of an enzyme in a metabolic pathway by an end product of that metabolic pathway
metabolic pathway
a process in which molecules are constructed or deconstructed. Precursor molecules are transformed in steps with an enzyme mediating each step, until the product is formed.
cooperativity
takes place when the binding of a substrate molecule to one subunit of an enzyme enhances the other subunits’ ability to accept substrate molecules
