Ap Bio - Chapter 3

Front 1

Global Warming

Back 1

A long-term rise in the lower atmosphere’s temperature

Front 2

Organic compounds

Back 2

Compounds containing carbon and at least one hydrogen atom.

Front 3

Hydrocarbons

Back 3

Compounds consisting of only carbon atoms covalently bonded to hydrogen (gas, fossil fuels, etc…)

Front 4

Functional groups

Back 4

Particular atoms or clusters of atoms covalently bonded to carbon.

Front 5

Carbon chains

Back 5

Backbones of molecules

Front 6

Methane

Back 6

Simplest hydrocarbon, CH4

Front 7

Ball-and-Stick Model

Back 7

Ball: atom, Stick: bond; Conveys bond angles and how mass is distributed.

Front 8

Space-Filling Model

Back 8

Conveys molecules mass and structural complexity.

Front 9

Ribbon Model

Back 9

Chains: strings of amino acids.

Front 10

Alcohols

Back 10

Have one or more hydroxyl groups (-OH) (sugars).

Front 11

Carbonyl groups

Back 11

Building blocks of fate and carbohydrates; highly reactive.

Front 12

Carboxyl groups

Back 12

Present in amino acids, fatty acids.

Front 13

Sulfhydryl group

Back 13

Component of cysteine helps stabilize structure of many proteins.

Front 14

Monomers

Back 14

Individual subunits of cells.

Front 15

Polynomers

Back 15

Larger molecules required for cell’s structure and functioning.

Front 16

Enzymes

Back 16

A class of proteins that make metabolic reactions proceed faster.

Front 17

Condensation

Back 17

Enzymes split off an –OH group from one molecule and an H atom from another so that the original molecules bond, -OH + H becomes H20

Front 18

Cleavage (Hydrolysis)

Back 18

Enzymes split molecules at specific groups then attach an -OH to one and an H to another (both from water).

Front 19

Carbohydrates

Back 19

Molecules consisting of carbon, hydrogen, and oxygen in a 1:2:1 ratio (CH2O)n; used as structural materials, transportable forms of energy in cells.

Front 20

Monosaccharide

Back 20

Simplest carbohydrates, at least two –OH groups and aldehyde/ketone; most dissolve easily in water.

Front 21

Glucose

Back 21

6 carbon atoms (mail energy source, backbone for others)

Front 22

Oligosaccharide

Back 22

Short chain of covalently bonded sugar monomers.

Front 23

Disaccharides

Back 23

Only two sugar units (e.g. lactose)

Front 24

Polysaccharides

Back 24

Straight or branched chains of many sugar monomers

Front 25

Cellulose

Back 25

Glucose chains stretch out side by side and bond at –OH --> stabilized chain, resists digestion (cell walls).

Front 26

Starch

Back 26

Glucose covalently bonds at angles --> coils like a spiral.

Front 27

Glycogen

Back 27

Animal’s equivalent of plants’ sugar-storage

Front 28

Lipids

Back 28

Nonpolar hydrocarbons

Front 29

Fats

Back 29

Lipids with one to three fatty acids attached to glycerol.

Front 30

Fatty acid

Back 30

Has up to 36 carbon atoms, a carboxyl group at one end, and hydrogen atoms occupying the rest or most of the remaining bonding sites.

Front 31

Triglycerides

Back 31

“Neutral” fats, three fatty acid tails attached to a glycerol unit.

Front 32

Phospholipids

Back 32

Glycerol backbone, two fatty acid tails, and a hydrophilic “head” with a phosphate group and another polar group.

Front 33

Sterols

Back 33

Lipids with no fatty acids, backbone of four fused carbon rings.

Front 34

Waxes

Back 34

Long-chain fatty acids linked to long-chain alcohols or carbon rings.

Front 35

Proteins

Back 35

The most diverse large biological molecules; do jobs.

Front 36

Amino Acid

Back 36

A small organic compound consisting of an amino group, a carboxyl group, a hydrogen atom, and one or more atoms known as the R group.

Front 37

Peptide Bonds

Back 37

Join successive amino acids when a cell synthesizes a protein

Front 38

Polypeptide Chain

Back 38

A chain of three or more amino acids joined by peptide bonds

Front 39

Fibrous Proteins

Back 39

Polypeptide chains in strands or sheets, contribute to cell’s shape or organization.

Front 40

Globular Proteins

Back 40

One or more chains folded, help cells and their parts move.

Front 41

Primary Structure

Back 41

One of twenty chosen amino acid sequences

Front 42

Secondary Structure

Back 42

How a polypeptide chain is structured (spiral, sheetlike, loops, etc…)

Front 43

Domain

Back 43

Polypeptide chain, or part of it, that has become self-organized as a structurally stable, functional unit.

Front 44

Tertiary Structure

Back 44

Domain formation.

Front 45

Quaternary structure

Back 45

Protein structure consisting of two or more polypeptide chains held together by hydrogen or covalent bonds.

Front 46

Denaturation

Back 46

The breaking of weak bonds of a protein or any other large molecule that disrupts its shape.

Front 47

ATP (Adenosine Triphosphate)

Back 47

String of three phosphate groups attached to sugar component; can transfer phosphate group to other molecules --> acceptor molecules are energized for reaction.

Front 48

Nucleic Acids

Back 48

Single and double-stranded molecules comprised of nucleotide monomers; covalent bond connects sugar compound of one nucleotide to a phosphate group of another.

Front 49

DNA

Back 49

Double-stranded molecules of deoxyribonucleic acid; passes out instructions for all other cells.

Front 50

RNA (Ribonucleic Acid)

Back 50

Consists of four kinds of nucleotide monomers; can carry DNA messeges.