Ap Bio Test 2

Front 1

Atomic number

Back 1

Number of protons

Front 2

Element

Back 2

Atoms that have the same atomic number and there fore have the same chemical properties

Front 3

Atomic Mass

Back 3

Sum of protons and neutrons

Front 4

Isotopes

Back 4

Atoms of the same element that have different atomic mass numbers due to different numbers of neutrons

Front 5

Neutral Atoms

Back 5

Have the same number of protons and electrons

Front 6

Ions

Back 6

Charged atoms

Front 7

Cations

Back 7

Have more protons than electrons and are positively charged

Front 8

Anions

Back 8

Have more electrons that protons and are negatively charged

Front 9

Oxidation

Back 9

Loss of an electron

Front 10

Reduction

Back 10

Gain of an electron

Front 11

Valence Electrons

Back 11

The electrons in the outermost energy level of an atom

Front 12

Periodic Table

Back 12

Arranges all elements according to their atomic number, and there fore organizes elements with similar chemical properties.

Front 13

Octet Rule

Back 13

Atoms tend to establish completely-full outer energy levels

Front 14

Molecules

Back 14

Groups of atoms held together in a stable group

Front 15

Compounds

Back 15

Molecules containing more than one type of element

Front 16

Chemical Bonds

Back 16

How atoms are held together in molecules or compounds

Front 17

Ionic Bonds

Back 17

Formed by the attraction of oppositely charged ions

Front 18

Covalent Bonds

Back 18

Form when atoms share 2 or more valence electrons. The strength depends on the number of electron pairs shared by the atoms

Front 19

Electronegativity

Back 19

An atom's affinity for electrons

Front 20

Nonpolar Covalent Bonds

Back 20

Equal sharing of electrons

Front 21

Polar Covalent Bonds

Back 21

Unequal sharing of electrons, delta slight charges. They are asymmetrically shared. O-H, N-H, N=C, O=C, S-H

Front 22

3 things that influence a chemical reaction:

Back 22

1. Temperature 2. Concentration of reactants and products 3. Availability of a catalyst (increases rate of chemical reaction)

Front 23

Hydrogen Bonds

Back 23

Weak attractions between the partially negative oxygen of one water molecule and the partially hydrogen of a different water molecule

Front 24

Cohesion

Back 24

Water molecules stick other water molecules by hydrogen bonding

Front 25

Adhesion

Back 25

Water molecules stick to other polar molecules by hydrogen bonding

Front 26

6 Properties of Water

Back 26

1. Has a high specific heat 2. Has a high heat of vaporization 3. Solid water is less dense than liquid water 4. A good solvent 5. Organizes nonpolar molecules 6. Can form ions

Front 27

Hydrophilic

Back 27

Water loving

Front 28

Hydrophobic

Back 28

Water fearing

Front 29

Acid

Back 29

A chemical that releases H+1 ions

Front 30

Base

Back 30

A chemical that accepts H+1 ions

Front 31

Buffer

Back 31

A chemical that accepts/releases as necessary to keep pH constant

Front 32

Amphipathic

Back 32

One side of a molecule is hydrophilic, and one is hydrophobic

Front 33

Dehydration Synthesis

Back 33

The formation of large molecules by the removal of water. Monomers are joined to make polymers

Front 34

Hydrolysis

Back 34

The breakdown of large molecules by the addition of water. Breaking 1 polymer back into 2 monomers

Front 35

Isomers

Back 35

Same molecular formula, different structure

Front 36

To be water soluble (2 things):

Back 36

1. Must be hydrophilic (Polar covalent bonds with delta charges or ionic, positive and negative) 2. Small

Front 37

Hydration Sphere

Back 37

Surrounded by a sphere of water molecules

Front 38

Functional Groups

Back 38

Carbon groups with specific properties

Front 39

Monomer

Back 39

Single subunity

Front 40

Polymer

Back 40

Many units

Front 41

Chiral

Back 41

Molecules are mirror-images of each other

Front 42

Monosaccharide

Back 42

A single sugar, contains 6 carbons, very important in energy storage, fructose is a structural isomer of glucose, and galactose is a stereoisomer of glucose. They are small and hydrophilic and can be carried through membranes

Front 43

Carbohydrates

Back 43

1. Available energy supply 2. Basic building block for polymers 3. Lots of OH's for dehydration synthesis

Front 44

Disaccharides

Back 44

Two monosacharides linked together by dehydration synthesis 1. Transport sugar/energy storage 2. Maintain osmotic balance ex. Sucrose, lactose

Front 45

Polysaccharides

Back 45

1. Long chains of sugars 2. Used for energy storage (Plants use starch, animals use glycogen) 3. Used for structural support 4. Plants use cellulose, animals use chitin

Front 46

Storage Polysaccharides

Back 46

1. Starch in plants stored in amloplasts of roots and seeds 2. Glycogen in animal's liver and muscles

Front 47

Structural Support Polysaccharides

Back 47

1. Cellulose in plants 2. Chitin in insect's exoskeletons and fungus cell walls 3. Peptoglycon in bacteria

Front 48

Functions of Nucleic Acids (DNA and RNA)

Back 48

The storage, transmission, and USE of genetic information and thus control the cell activity and characteristics by controlling what proteins are made

Front 49

Nucleotides

Back 49

Sugar + phosphate + nitrogenous base

Front 50

Purines

Back 50

Adenine and Guanine

Front 51

Pyrimadines

Back 51

Thymine (DNA), Cytosine, Uracil (RNA)

Front 52

Phosphodiester Bonds

Back 52

Connect nucleotides

Front 53

Double Helix

Back 53

2 polynucleotide strands connected by hydrogen bonds

Front 54

DNA

Back 54

1. Phosphodiester bonds 2. Double helix 3. Strands are complimentary 4. Genetic information is carried in a sequence of nucleotides

Front 55

RNA

Back 55

1. Contains Ribose instead of deoxyribose 2. Contains Uracil instead of Thymine 3. Single polynucleotide strand

Front 56

Functions of RNA

Back 56

1. Read the genetic information in DNA 2. Direct the synthesis of proteins (rRNA, tRNA, mRNA)

Front 57

ATP

Back 57

Primary energy currency of the cell

Front 58

NAD+ and FAD

Back 58

Electron carriers for many cellular reactions

Front 59

7 Protein Functions

Back 59

1. Enzyme catalysts (Callotripsen) 2. Defense (antibodies/antigens) 3. Transport (Carry Oxygen) 4. Support (Callogen has to have the right shape) 5. Motion (Actin and Myesin in muscles) 6. Regulation (Hormones and neurotransmitters) 7. Storage

Front 60

Amino Acids

Back 60

20 different ones, joined by dehydration synthesis, and have peptide bonds

Front 61

Peptide Bonds

Back 61

Form between adjacent amino acids

Front 62

Amino Acids are classified as:

Back 62

1. Nonpolar 2. Polar 3. Charged 4. Aromatic 5. Special function

Front 63

Primary Structure of proteins

Back 63

Sequence of amino acids

Front 64

Secondary structures of proteins

Back 64

Interaction of groups in the peptide backbone ex. Helix, sheet, tertiary structure, and quaternary structure

Front 65

Chaperone Proteins

Back 65

Help fold the proteins

Front 66

Denaturation

Back 66

A change in the shape of a protein, causing a loss of function. It may involve complete unfolding of the protein and is caused by changes in the protein's environment (pH, temperature, and salt concentration)

Front 67

Lipids

Back 67

A group of molecules that are insoluble in water. A high proportion of nonpolar C-H bonds causes the molecule to be hydrophobic. Two main categories: Fats and phopholipids

Front 68

Triglycerides

Back 68

Have 1 glycerol + 3 fatty acids

Front 69

Fatty Acids

Back 69

Are long hydrocarbon chains which may be either: saturated, unsaturated, or polyunsaturated

Front 70

Triglycerides

Back 70

1. An excellent molecule for energy storage 2. Stores 2x as much energy as carbohydrates 3. Animal fats are saturated fats 4. Plant fats (oils) are unsaturated

Front 71

Phospholipids are composed of:

Back 71

1 glycerol, 2 fatty acids, and a phosphate group

Front 72

Micelles/Lipid Bilayers

Back 72

Phospholipids form them and they are structures that cluster the hydrophobic regions of the phospholipid toward the inside and leave the hydrophilic regions exposed to the water environment. They are the basis of membranes

Front 73

Energy

Back 73

The capacity to do work

Front 74

Kinetic Energy

Back 74

The energy of motion

Front 75

Potential Energy

Back 75

Stored energy

Front 76

Kilocalories

Back 76

What heat is measured in

Front 77

Calorie

Back 77

The amount of heat required to raise the temperature of water by 1 degree C.

Front 78

Oxidation

Back 78

Loss of electrons

Front 79

Reduction

Back 79

Gain of electrons

Front 80

Redox Reactions

Back 80

Are coupled to each other

Front 81

First Law of Thermodynamics

Back 81

Energy cannot be created or destroyed. It can be used for transferring, changing, and storing. Energy can only be converted from one form to another

Front 82

Second Law of Thermodynamics

Back 82

Entropy (disorder in the universe) is always increasing more than order

Front 83

Free Energy

Back 83

The energy AVAILABLE to do work (has the symbol G)

Front 84

Enthalpy

Back 84

Energy contained in a molecule's chemical bonds

Front 85

Endergonic Reaction

Back 85

A reaction requiring an input of energy (DG is positive)

Front 86

Exergonic Reaction

Back 86

A reaction that releases free energy (DG is negative)

Front 87

Activation Energy

Back 87

Extra energy needed to get a reaction started. It destabilizes chemical bonds and requires exergonic reactions

Front 88

Catalysts

Back 88

Substances that lower the activation energy of a reaction

Front 89

Enzymes

Back 89

Molecules that catalyze reactions in living cells

Front 90

Substrate

Back 90

Molecules that will undergo a reaction

Front 91

Active Site

Back 91

Region of the enzyme that binds to the substrate

Front 92

3 Ways that Enzymes are Thrifty Nifty Neat

Back 92

1. Specific 2. Reusable 3. Lower the amount of energy (Bringing reactants together, and putting on pressure)

Front 93

Ribozymes

Back 93

RNA with enzymatic abilities

Front 94

Inhibitors

Back 94

Molecules that bind to an enzyme to decrease enzyme activity

Front 95

Competitive Inhibitors

Back 95

Compete with the substrate for binding to the same active site

Front 96

Noncompetitive Inhibitors

Back 96

Bind to sites other than the enzyme's active site

Front 97

Allosteric Enzymes

Back 97

Exist in either an active or inactive state

Front 98

Allosteric Site

Back 98

Where molecules other than the substrate bind

Front 99

Allosteric Inhibitors

Back 99

Bind to the allosteric site to inactivate the enzyme

Front 100

Allosteric Activators

Back 100

Bind to the allosteric site to activate the enzymes

Front 101

Metabolism

Back 101

All chemical reactions occuring in an organism

Front 102

Anabolism

Back 102

Chemical reactions that expend energy to make new chemical bonds

Front 103

Catabolism

Back 103

Chemical reactions that harvest energy when bonds are broken

Front 104

Cofactors

Back 104

Metal ions, found in the active site in catalysts

Front 105

Coenzymes

Back 105

Nonprotein organic molecules, ofter used as an electron donor or acceptor in a redox reaction

Front 106

Biochemical Pathways

Back 106

A sense of reactions in which the product of one reaction becomes the substrate for the next reaction.

Front 107

Feedback Inhibition

Back 107

The end product of the pathway is an allosteric inhibitor of an earlier enzyme in the pathway.