Chapter 2: Inorganic and Organic Chemistry Flashcards Preview

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Flashcards in Chapter 2: Inorganic and Organic Chemistry Deck (97):
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ion

a charged atom

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ionization

the formation of ions by loss of electrons

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Lewis Dot notation

a form of electron notation that involves only drawing the valence electrons

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isotope

an atom that has a different number of neutrons than other atoms with the same atomic number

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radioisotopes

radioactive isotopes

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atomic mass

the number of neutrons plus the number of protons

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Van Der Waal's interactions

weak interactions between regions of nonpolar molecules, resulting from charge fluctuations within molecules

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electronegativity

the measure of an atom’s tendency to hold or gain electrons

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electrostatics

describes the tendency for positive and negative charges to attract

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ionic bonds

form from the attraction of the oppositely charged ions

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covalent bonds

form when the differences between the electronegativities of atoms are equal or similar

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polar covalent bonds

 result when one atom in a covalent bond is more electronegative than the other

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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

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solvent

a fluid in which molecules dissolve

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dissociation

the breaking apart of molecules

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specific heat

the amount of heat needed to raise the temperature of one gram by one degree Celsius

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solubility

a substance's ability to dissolve other substances

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hydration shells

the result of separating ions from each other in a water molecule

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adhesion

the property of water to cling to other materials because of its ability to form hydrogen-bonds

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cohesion

the property of water to cling to other water molecules because of its ability to form hydrogen-bonds

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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

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turnover

the process of water on the surface sinking as it approaches 4 degrees Celsius, and drawing up warmer water from the bottom

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hydrophobic

water fearing

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hydrophilic

water loving

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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.

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acid

a proton donor

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base

a proton acceptor

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buffer

a substance that helps to maintain a constant pH

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organic chemistry

the chemistry of carbon-containing molecules

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structural isomers or constitutional isomers

molecules that have the same formula, but whose atoms are arranged differently

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geometric isomers

molecules that have the same formula, but have atoms arranged differently about a double bond

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Enantiomers

isomers that are mirror images of each other and are not superimposable

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functional side groups

parts of organic molecules that have their own characteristic properties

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the hydroxyl group

consists of an —OH

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carbonyl group

consists of an oxygen atom double-bonded to a carbon atom (CO)

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carboxyl group

consists of a carbon with a double-bonded oxygen atom and a hydroxyl group (COOH)

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amine group

consists of an —NH2 group

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carbohydrates

macromolecules that play a role in energy storage and structure

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monosaccharides

simple one-sugar molecules that consist of carbon, hydrogen, and oxygen

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trioses

three-carbon monosaccharides

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pentoses

five-carbon monosaccharides

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hexoses

six-carbon monosaccharides

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dehydration synthesis

the process by which two monosaccharides are linked together to form a disaccharide

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hydrolysis

the process by which a disaccharide is separated into two monosaccharides

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monomer

a subunit of a polymer

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glycosidic linkage

the bond between monosaccharides

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lipids

molecules that are nonpolar and insoluble in water

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fatty acid

a carboxylic acid consisting of a hydrocarbon chain and a terminal carboxyl group

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ester linkage

the linkage between a fatty acid and glycerol molecule in a triglyceride

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respiration

the process by which the energy stored in triglyceride bonds in released

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saturated fatty acid

a fatty acid that has as many hydrogen atoms as possible on the carbon chain

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unsaturated fatty acid

a fatty acid that has double bonds within the carbon chain, and therefore fewer hydrogen atoms

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phospholipid

a type of lipid that has a hydrophilic, polar head, and hydrophobic, nonpolar tails

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steroids

lipids that consist of four fused carbon rings

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waxes

lipids that make up leaf cuticles and organ protective filters

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nucleotides

the subunits of polymers

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purines

two-ringed molecules that include adenine and guanine

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pyrimidines

one-ringed molecules that include cytosine, thymine, and uracil

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deoxyribose

the pentose sugar that makes up the nucleotides of DNA

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ribose

the pentose sugar that makes up the nucleotides of RNA

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what is the central dogma of biology?

DNA makes RNA, which makes proteins

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conformation

the specific shape of a protein, as determined by its primary structure

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R group

a group in which a carbon or hydrogen atom is attached to the rest of the molecule

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peptide bond

a bond between amino acids, which is formed by dehyration synthesis

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polypeptide

a chain of amino acids bonded together, with an amine group on one end and a carboxyl group on the other

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what are the charged amino acids?

AGLAH: aspartic acid, glutamic acid, lysine, arginine, histidine

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what are the polar amino acids?

CATTGS: cysteine, asparagine, tyrosine, threonine, glutamine, serine

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what are the nonpolar amino acids?

PALM PIG TV: phenylalanine, alanine, methionine, proline, isoleucine, glycine, tryptophan, valine

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primary structure

the specific sequence of amino acids in a polypeptide

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secondary structure

the regular pattern of local hydrogen bonding within the polypeptide chain

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tertiary structure

three-dimensional folding that results from interactions between R groups

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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

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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

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ionic bonding (between R groups)

tertiary structure interactions that occur between R groups of opposite charges

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disulfide bridges

teritary structure interactions that result in strong covalent bonds that form between two sulfhydril groups of cysteine

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quaternary structure

the final structure of a protein that results from interactions between polypeptides

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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

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the first law of thermodynamics

energy can neither be created nor destroyed

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the second law of thermodynamics

every energy transfer results in an increase in entropy

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entropy

the measure of randomness or disorder in a system

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exergonic reaction

a reaction that has a negative amount of free energy, and thus gives off energy

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catabolism

all of the metabolic processes that give off energy, and involves the breakdown of molecules

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anabolism

all of the metabolic processes that require an input of energy. These reactions typically involve the synthesis of new molecules.

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energy coupling

the process by which energy released from an exergonic reaction is used to feul an endergonic one

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activation energy

the energy required to start the reaction

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enzymes

proteins that serve as catalysts of biological reactions

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endergonic reaction

a reaction that has a positive amount of free energy, and thus requires energy to be put into it to function 

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induced-fit model

the hypothesis for enzyme action, where the substrate induces a more complete fit of the enzyme's active site around it

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competitive inhibitor

an inhibitor that competes with the substrate for the active site

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noncompetitive inhibitor

an inhibitor than can bind to a part of the enzyme other than the active site permanently, ceasing that enzyme's function

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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

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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)

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allosteric activator

an activator that binds to the enzyme and keeps it in an active state, where the active site is exposed

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allosteric inhibitor

an inhibitor that binds to the enzyme and keeps it in an inative state, where the active site is inaccessable

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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

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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.

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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