Ap Biology Cliffnotes Chp 1

Front 1

consists of a nucleus of positively charged protons and neutrally charged neutrons

Back 1

atom

Front 2

are groups of two or more atoms held together by chemical bonds

Back 2

molecules

Front 3

ability of an atom to attract electrons

Back 3

electronegativity

Front 4

What are three kinds of atomic bonds?

Back 4

ionic, covalent, hydrogen

Front 5

bonds form between two atoms when one or more electrons are transferred from one atom to the other

Back 5

ionic

Front 6

bond with the highest electronegativity

Back 6

ionic

Front 7

atoms with positive or negative charges

Back 7

ions

Front 8

bonds form when electrons between atoms are shared

Back 8

covalent

Front 9

What are two types of covalent bonds?

Back 9

nonpolar and polar

Front 10

bonds form when electrons are shared equally

Back 10

nonpolar covalent

Front 11

bonds form when electrons are shared unequally

Back 11

polar covalent

Front 12

negative charge

Back 12

pole

Front 13

In a polar covalent bond, which atom has the stronger pull?

Back 13

the one with the highest

Front 14

are weak bonds between molecules

Back 14

hydrogen bonds

Front 15

What are the five properties of water?

Back 15

-is an excellent solvent
-has a high capacity
-ice floats
-strong cohesion and high surface tension
-has strong adhesion

Front 16

Which two bonds are soluble?

Back 16

polar covalent and ionic

Front 17

What bond is hydrophobic?

Back 17

nonpolar covalent

Front 18

is the degree to which a substance changes temperature in response to gain or loss of heat

Back 18

heat capacity

Front 19

What is does water do when it freezes?

Back 19

water expands

Front 20

attraction between like substances

Back 20

cohesion

Front 21

What does the strong cohesion in water create?

Back 21

surface tension

Front 22

is the attraction of unlike substance

Back 22

adhesion

Front 23

water adheres to the walls of narrow tubing or to absorbent solids like paper

Back 23

capillary action

Front 24

molecules that have carbon atoms

Back 24

organic molecules

Front 25

large organic molecules

Back 25

macromolecules

Front 26

most macromolecules are

Back 26

polymers

Front 27

molecules that consist of a single unit repeated many times

Back 27

polymers

Front 28

single unit of a polymer

Back 28

monomer

Front 29

clusters of atoms that give molecules their properties

Back 29

functional groups

Front 30

What are the three groups of carbohydrates

Back 30

monosaccharide
disaccharide
polysaccharide

Front 31

is the simplest kind of carbohydrate

Back 31

monosaccharide

Front 32

consists of two sugar molecules joined by a glycodic linkage

Back 32

dissacharide

Front 33

a chemical reaction where a simple molecule (more often water) is lost

Back 33

condesation synthesis

Front 34

glucose + fructose =

Back 34

sucrose

Front 35

glucose + galactose =

Back 35

lactose

Front 36

glucose + glucose =

Back 36

maltose

Front 37

consists of a series of connected monosaccharides

Back 37

polysaccharide

Front 38

is a polymer of alpha glucose molecules. is the principal energy storage molecule in plant cells

Back 38

starch

Front 39

is a polymer of alpha molecules. major energy storage molecule in animal cells

Back 39

glycogen

Front 40

is a polymer of beta glucose. it serves as a structural molecule in plant cells

Back 40

cellulose

Front 41

is a polymer of beta glucose. serves as a structural molecule for animal cells

Back 41

chitin

Front 42

What are the three major types of lipids?

Back 42

Triglycerides
phospholipid
steroids

Front 43

glycerol + 3 fatty acids =

Back 43

triglyceride

Front 44

What are three types of fatty acids?

Back 44

saturated
monounsaturated
polyunsaturated

Front 45

fatty acid that has a single covalent bond between each carbon atom and each carbon has two hydrogens bonded to it

Back 45

saturated

Front 46

fatty acid that has one double covalent bond and each of the two carbons in this bond has only one hyrogen atom bonded to it

Back 46

monounsaturated

Front 47

fatty acid that has two or more double covalent bonds

Back 47

polyunsaturated

Front 48

looks like a lipid except that one of the fatty acid chains is replaced by a phsophate group

Back 48

phospholipid

Front 49

has both polar and nonpolar regions

Back 49

amphipathic molecules

Front 50

are characterized by a backbone of four linked carbon rings

Back 50

steroids

Front 51

What are some major categories for proteins?

Back 51

structural, storage, transport, defensive, and enzymes

Front 52

all proteins are polymers of what?

Back 52

amino acids

Front 53

the bonds between amino acids

Back 53

peptide bonds

Front 54

the chain of amino acids is called

Back 54

polypeptide

Front 55

What does a basic amino acid structure look like?

Back 55

central carbon with an amino group, carboxyl group, and an R group

Front 56

What factors contribute to a tertiary structure of a protein?

Back 56

hydrogen bonding
ionic bonding
hydrophobic effect
formation disulfide bonds

Front 57

occurs when hydrophobic R groups move toward the center of a protein (away from the water that the protein is emmersed in)

Back 57

hydrophobic effect

Front 58

when the sulfur atom in the amino acid cysteine bonds to the sulfur atom in another cysteine

Back 58

disulfide bonds

Front 59

What does a DNA nucleotide consist of?

Back 59

nitrogen base
deoxyribose
phosphate group

Front 60

What aer the four nitrogen bases?

Back 60

Adenine
Thymine
Cytosine
Guanine

Front 61

What are the purines?

Back 61

adenine and guanine

Front 62

What are the pyrimidines?

Back 62

thymine and cytosine

Front 63

What are three ways in which RNA differs from DNA?

Back 63

-RNA has ribose
-thymine is replaced by uracil
-is single stranded and doesn't form a double helix

Front 64

sufficient energy to form new bonds

Back 64

activation energy

Front 65

accelerates the rate of the reaction because it lowers the activation energy required for the reaction to take place

Back 65

catalyst

Front 66

the breakdown of substances

Back 66

catabolism

Front 67

formation of new products

Back 67

synthesis (anabolism)

Front 68

What determines whether a reaction proceeds forward or backward?

Back 68

concentration of reactants and end products

Front 69

describes the condition where the rate of reaction in the forward direction equals the rate in the reverse direction and there is no net production of reactants or products

Back 69

equlibrium

Front 70

is the substance or substances upon which the enzyme acts

Back 70

substrate

Front 71

lose 3d shape as hydrogen bonds and peptide bonds begin to break down

Back 71

denatured

Front 72

describes how enzymes work

Back 72

induced-fit model

Front 73

nonprotein molecules that assist enzymes

Back 73

cofactors

Front 74

is the union of the cofactor and the enzyme

Back 74

holoenzyme

Front 75

are organic cofactors that usually function to donate or accept some component of a reaction

Back 75

coenzymes

Front 76

is a common source of activation energy for metabolic reactions

Back 76

ATP

Front 77

ADP combines with a phosphate group using energy obtained from some energy-rich molecule

Back 77

phosphorylation

Front 78

What are the two kinds of allosteric effector?

Back 78

Allosteric activator
Allosteric activator

Front 79

binds the enzyme and induces the enzyme's active form

Back 79

allosteric activator

Front 80

binds to the enzyme and induces the enzyme's inactive form

Back 80

allosteric inhibitor

Front 81

a substance that mimics the substrate inhibits an enzyme by occupying the active site

Back 81

competetive inhibition

Front 82

an enzyme becomes more receptive to additional substrate molecules after one substrate molecule attaches to an active site

Back 82

cooperativity