Cliff's Ap Biology Vocabulary: Chemistry

Front 1

Atoms

Back 1

consist of positively charges protons and neutrally charged neutrons with negatively charged electrons arranged outside the nucleus

Front 2

Molecules

Back 2

groups of two or more atoms held together by chemical bonds

Front 3

Chemical Bonds

Back 3

interaction of electrons

Front 4

Electronegativity

Back 4

ability of an atom to attract electrons

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Ionic Bond

Back 5

when one or more electrons are transferred from one atom to the other or when there is a large difference in electronegativities.

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Covalent Bond

Back 6

forms when electrons are shared

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Non-polar Covalent Bond

Back 7

forms when electrons are shared equally

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Polar-covalent

Back 8

forms when electrons are shared unequally

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Pole

Back 9

When electrons form a bond around the atom with greater electronegativity, a negative charge is produced. Also known as a pole.

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Hydrogen Bonds

Back 10

Weak bonds that form between two molecules when a positively charged hydrogen atom is attracted to a negatively charged area of another atom.

Front 11

Why is water a good solvent?

Back 11

Polar water molecules can interact with ionic substances and separate them into ions.

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Hydrophilic

Back 12

"Water Loving."

Front 13

Hydrophobic

Back 13

"Water Fearing." Substances that lack charged poles do not dissolve in water and are thus hydrophobic.

Front 14

Define Heat Capacity and describe why it is beneficial for water to have a high heat capacity.

Back 14

Heat Capacity is the degree to which a substance changes temperature in response to a gain or loss of heat. Water has a high heat capacity, which means that its temperature changes very slowly and that it takes a lot of energy to heat or cool water.

Front 15

Why does ice float?

Back 15

water expands as it freezes, thus it is more dense in the solid form.

Front 16

Define Cohesion and describe why water has strong cohesion.

Back 16

Cohesion is the attraction between like substances and the hydrogen bonds in water are what give water its strong cohesion, eventually giving it high surface tension.

Front 17

Adhesion

Back 17

attraction of unlike substances

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Capillary Action

Back 18

Water displays capillary action by rising up tubing or creeping through paper.

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OH

Back 19

hydroxyl group - polar and hydrophilic

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COOH

Back 20

Carboxyl group - polar and hydrophilic

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NH2

Back 21

amino group - polar and hydrophilic

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PO3 2-

Back 22

Phosphate group - polar and hydrophilic

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CO (end)

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Carbonyl (Ketone)

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CO (Middle)

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Carbonyl (Aldehyde)

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CH3

Back 25

Methyl - nonpolar and hydrophobic

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Name the three divisions of carbohydrates

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Monosaccharides, Disacharides, and Polysaccharides

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Monosacharride

Back 27

single sugar molecule with the formula (CH20)n

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Disacharrides

Back 28

two sugar molecules

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Glycosidic Linkage

Back 29

bond between two sugars that results in the loss of water (aka dehydration reaction)

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Polysacharride

Back 30

a series of monosacharrides

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Starch

Back 31

polymer of alpha glucose. Serves as energy storage in plants

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Glycogen

Back 32

polymer of alpha glucose. Serves as energy storage in animals. Branching is different that starch.

Front 33

Cellulose

Back 33

polymer of beta glucose. Serves as a structural molecule in plant cell walls.

Front 34

Chitin

Back 34

polymer of beta glucose, but has a nitrogen group attached to the ring. Serves as a structural molecule in the walls of fungus or exoskeletons of insects.

Front 35

Describe some properties of lipids and name the three main groups of lipids

Back 35

Lipids are insoluble in water. Three main groups are triglycerides, phospholipids, and steroids

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Triglycerides

Back 36

consist of three fatty acids attached to a glycerol molecule

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Saturated Fatty Acid

Back 37

has a single covalent bond between each pair of carbon atoms.

Front 38

Monounsaturated Fatty Acid

Back 38

has one double covalent bond

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Polyunsaturated Fatty Acid

Back 39

has two or more double covalent bonds

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Phospholipid

Back 40

looks like a lipid except one of the fatty acid chains is replaced with a phosphate group, thus there is a phosphate "head" and fatty acid "tails"

Front 41

Amphipatic

Back 41

has both polar and nonpolar regions

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Steroids

Back 42

contain a backbone of four linked carbon rings

Front 43

Name 5 Major protein categories

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Structural, Storage, Transport, Defensive, and Enzymes

Front 44

What are proteins?

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Proteins, also known as polypeptides, are polymers of amino acids held together by peptide bonds

Front 45

What is the structure of an amino acid?

Back 45

A central carbon bonded to an amino group, a carboxyl group, a hydrogen, and a functional R group

Front 46

Primary Structure of Proteins

Back 46

order of amino acids

Front 47

Secondary Structure of Proteins

Back 47

3D shape formed from hydrogen bonds between amino and carboxyl groups of adjacent amino acids. Most secondary structures result in the alpha helix or beta pleated sheet.

Front 48

Fibrous Proteins

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Proteins dominated by either the alpha helix or beta pleated sheet structures.

Front 49

Tertiary Structure of Proteins

Back 49

additional 3D shaping aqnd often dominates the structure of globular proteins

Front 50

What factors contribute to tertiary structure?

Back 50

Hydrogen Bonding, Ionic Bonding, Hydrophobic Effect (when hydrophobic R groups move toward the center), and formation of disulfide bonds.

Front 51

Quaternary Structure

Back 51

protein that is assembled from two or more polypeptide chains

Front 52

What is DNA?

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Also known as Deoxyribonucleic Acid, DNA is a polymer of nucleotides

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What do nucleotides consist of?

Back 53

Nitrogen base, five carbon sugar (deoxyribose), and a phosphate group

Front 54

Name the 4 DNA nucleotides?

Back 54

Adenine, Thymine, Cytosine, Guanine

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Pyrimidine

Back 55

single ring sugar base

Front 56

Purine

Back 56

double ring sugar base

Front 57

What is the grouping of the nucleotides? That is, which can bond to which?

Back 57

Adenine and Thymine, Cytosine and Guanine

Front 58

What does it mean for DNA to be antiparallel?

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Antiparallel means that each strand is oriented in opposite directions, one is from the 5'-->3' direction while the other is 3'-->5'

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How does RNA differ from DNA?

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the sugar is ribose, thymine does not exist in RNA, it is replaced with uracil, and it is single stranded

Front 60

Activation Energy

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Energy required to trigger thr formation of new bonds

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Catalyst

Back 61

lowers the activation energy required for a reaction to take place

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Metabolism

Back 62

chemical reactions that occur in biological systems

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Catabolism

Back 63

the breakdown of substances

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Synthesis

Back 64

formation of new products

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Anabolism

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formation of new products

Front 66

Equilibrium

Back 66

when the rate of the forward reaction equals the rate of the reverse reaction

Front 67

Enzymes

Back 67

globular proteins that act as catalysts for metabolic reactions

Front 68

Substrate

Back 68

substance(s) upon which the enzyme acts

Front 69

Induced Fit Model (Lock and Key)

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within the enzyme, there is an active site with which reactants readily interact because of the shape, polarity, or other characteristics of the active site.

Front 70

What two factors cause enzymes to lose their functionality?

Back 70

Temperature and pH

Front 71

What is the standard suffix for enzymes?

Back 71

ase

Front 72

Cofactors

Back 72

nonprotein molecules that assist enzymes

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Holoenzyme

Back 73

union of cofactor and enzyme (apoenzyme when joined together)

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Coenzyme

Back 74

organic cofactors that usually function to donate or accept some component of the reaction, often electrons

Front 75

Inorganic Cofactors

Back 75

often metal ions

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ATP

Back 76

Adenosine Triphosphate is a common source of activation energy for metabolic reactions

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Phosphorylation

Back 77

when new ATP molecules are assembled via ADP+phosphate

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What is an allosteric enzyme and describe its function

Back 78

they help regulate chemical reactions. They have two binding sites, an active site for substrates and an allosteric site for an allosteric effector

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Allosteric Activator

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binds to the enzyme and induces the enzymes active form

Front 80

Allosteric Inhibitor

Back 80

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

Front 81

Feedback Inhibition

Back 81

an end product of a series of reactions that acts like an allosteric inhibitor

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Competitve Inhibition

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substance that mimics the substrate and occupies the active site

Front 83

Noncompetitive Inhibitor

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binds to an enzyme at locations other than an active or allosteric site and causes the enzyme to change shape and lose functionality

Front 84

Cooperativity

Back 84

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