Biology 12 Unit 1

Front 1

moleules

Back 1

atoms arranged in fixed ratios

Front 2

compounds

Back 2

elements combined together in fixed rations, held together by chemical bonds

Front 3

orbital

Back 3

Region of space that is occupied by electrons located around the nucleus of an atom

Front 4

energy levels

Back 4

Within the orbital. Also known as energy shells and are numbered as 123 excetera.

Front 5

The further away an electron is from the nucleus

Back 5

The greater the energy

Front 6

Inert atoms

Back 6

They have a complete octet sand are non active

Front 7

Cation

Back 7

Ion with a positive charge

Front 8

anion

Back 8

Ion with a negative charge

Front 9

What determines the strength of covalent bonds

Back 9

The electronegativity of each atom

Front 10

Electronegativity

Back 10

The measure of an atom's attraction to share electrons

Front 11

Polar covalent bonds

Back 11

A bond between two atoms. Made up of unequally shared electrons

Front 12

Polarity

Back 12

Partial positive or negative charge at the ends of a molecule

Front 13

Electronegativity distance

Back 13

Below 0.4 is nonpolar covalent.

before 1.8 is polar covalent.

After 1.8 it's an ionic bond

Front 14

Intermolecular force

Back 14

Force of attraction between two molecules

Front 15

Van Der waals forces

Back 15

Very weak attraction between two molecules or parts of molecules when they're close together. London Force, dipole dipole Force, hydrogen bonding

Front 16

Water is the

Back 16

Universal solvent. More substances dissolve in water than anything else

Front 17

Properties of water

Back 17

Special because it's size, shape, polar structure, and ability to associate with each other because of hydrogen bonding.

Hydrogen bonds between water constantly break and reform new positions.

The fluid property is created by the lattice it forms between the molecules

Front 18

How is ice created

Back 18

When the water lattice becomes a rigid crystalline structure

Front 19

Specific heat

Back 19

The amount of thermal energy required to raise the temperature of a given quantity of a substance by 1 degrees Celsius

Front 20

Up until how many degrees does water stay liquid

Back 20

0 to 100 degrees

Front 21

Property of adhesion

Back 21

Occurs between water molecules and other polar molecules

Front 22

Cohesion

Back 22

Create surface tension, which is the measure of how difficult it is to stretch or break the surface of a liquid

Front 23

Hydrophilic molecules

Back 23

Polar or charged molecules that are strongly attracted to water

Front 24

Hydrophobic molecules

Back 24

Nonpolar molecules that are not attracted to water

Front 25

Why can cells in blood carry out the reactions they do

Back 25

They are made up of water molecules which means they can dissolve thousands of solutes necessary for life

Front 26

Autoionization

Back 26

Process in which air molecules spontaneously dissociates into ions

Front 27

What happens when water reacts with itself

Back 27

Forms hydronium ions, h3o + oh, and hydroxide, oh -. There's an equal amount of each

When the concentration is altered acids and bases are created

Front 28

When there's more hydronium ions

Back 28

An acid is created

Front 29

When there are more hydroxide ions

Back 29

A base is created

Front 30

What does the strength of an acid or base depend on

Back 30

The degree to which it ionizes when dissolved in water. Strong acids and bases are completely dissociated in water, creating an aqueous solution

Front 31

Hydrocarbon

Back 31

Molecules that are made up of a carbon and hydrogen atoms. For example methane, CH4

Front 32

Organic molecules

Back 32

Molecules consisting of a carbon chain, with hydrogen and other atoms (nitrogen oxygen and sulphur) attached

Front 33

Why can carbon form the backbone of large diverse molecules

Back 33

Carbon's ability to form bonds like for covalent bonds

Front 34

Why is carbon bonding unique

Back 34

It has the ability to form four single covalent bonds but may also form double and triple covalent bonds

Front 35

Is the lipid molecule a polymer

Back 35

No but it is composed of subunits glycerol and fatty acid chains

Front 36

Functional group

Back 36

A group of atoms that affects the function of a molecule by participating in chemical reactions.

Usually strongly polar or ionic.

They form small reactive groups which allow organic molecules to undergo synthesis and dehydration

Front 37

Hydroxyl group

Back 37

Oh. Alcohol, ethyl alcohol

Front 38

carbonyl group

Back 38

=o, aldehyde, acetaldehyde

Front 39

carboxyl group

Back 39

(COOH) krganic acids, acetic acid

Front 40

amino group

Back 40

NH2, amino acids, alanine

Front 41

phosphate

Back 41

po4, nucleic acids, glyeraldehydes-3-phosphate

Front 42

sulfhydryl

Back 42

sh, cellular molecules, merceptoethanol

Front 43

Dehydration and hydrolysis

Back 43

H+ and O H - ions are gained or lost from organic molecules. Dehydration is the removal of water usually during the building of a larger molecule from smaller subunits.

Front 44

Carbohydrates

Back 44

Consists of carbon, oxygen, and hydrogen. Most common biomolecule on Earth. Needed by all living things, photosynthesis or cellular respiration

Front 45

Function of carbohydrates

Back 45

Primary energy source of the cells and also use as a structural component of cells and organisms

Front 46

Monosaccharides

Back 46

Made of six carbons and are isomers of each other. Consists of a single sugar unit. Building block for more complex carbs.

Front 47

Types of monosaccharides

Back 47

Glucose galactose and fructose

Front 48

Triose

Back 48

Monosaccharide with 3 carbons. Glyceraldehyde

Front 49

Pentose

Back 49

Monosaccharide with 5 carbons. Ribose

Front 50

Hexose

Back 50

Monosaccharide with 6 carbons. Glucose

Front 51

Formula for simple sugar molecules

Back 51

C6 h-12 o-6

Front 52

Glucose appearance

Back 52

A linear molecule but in the presence of water it becomes rings as the functional groups hydroxyl and carbonyl interact

Front 53

Alpha glucose and beta glucose

Back 53

When glucose forms a ring there's two possible Arrangements when the oah group attaches to the carbon deposition one. There are isomers of each other

Front 54

Isomer

Back 54

A molecule that has the same composition as another but a different arrangement of atoms

Front 55

Alpha glucose

Back 55

Starch

Front 56

Beta glucose

Back 56

Cellulose

Front 57

Disaccharides

Back 57

Created when two monosaccharides are bonded together through a dehydration reaction.

Front 58

Types of disaccharides

Back 58

Maltose lactose and sucrose

Front 59

How is maltose created

Back 59

When two glucose molecules form a glycosidic bond between the o h group on carbon position of one glucose and the o h group on carbon position for of another glucose

Front 60

Glycosidic Bond

Back 60

Bond between two monosaccharides

Front 61

What is the linkage of saccharides determined by

Back 61

The orientation of the o h group to the carbon position 1

Front 62

Complex carbohydrates

Back 62

Important energy storage and structural molecules, depending on the amount of monosaccharides that make up the chain

Front 63

Energy storage versus structural complex carbs

Back 63

Energy storage and chitin / cellulose

Front 64

What are complex carbs made

Back 64

Hundreds to thousands of monosaccharides linked together. An essential part of nutrition into valuable energy source

Front 65

Macromolecules

Back 65

Made up of many monosaccharide subunits bonded together glycosidic bonds through a dehydration reaction

Front 66

Polysaccharide

Back 66

Many linked monosaccharides. This is a polymerization reaction

Front 67

Polymerization

Back 67

Process in which small subunits are linked to form one large molecule

Front 68

Types of polysaccharides

Back 68

Cellulose which is structural,

starch which is an energy source in plants,

glycogen which is an energy source in animals from the digestion of starch,

Front 69

Monomer

Back 69

Small molecule that can bind chemically to other molecules

Front 70

Polymer

Back 70

Large molecule that is formed when monomers linked together chemically in a chain

Front 71

Lipids

Back 71

Nonpolar molecules composed mostly of carbon and hydrogen in some oxygen. Insoluble in water. Not polymers because they are not made of repeating subunits

Front 72

Function of lipids

Back 72

Secondary energy source for the cell and a structural component of cells, hormones, certain vitamins, immune response, isolation, and Waterproofing

Front 73

Fatty acids

Back 73

Molecule that consists of a carboxyl group and a hydrocarbon chain. They have a single hydrocarbon chain with the carboxyl on one end.

The carboxyl allows change interact with other molecules and gives it acidic properties

Front 74

Fatty acid chain

Back 74

Consists of four or more carbons in the hydrocarbon backbone. Most common forms have an even number of carbons ranging from 14 to 22

Front 75

Saturated chains

Back 75

Carbon bonded together by single covalent bonds

Front 76

Unsaturated chains

Back 76

Have one or more double covalent bonds between carbons making up the chain

Front 77

Mono saturated chains

Back 77

Have only one double covalent bonds in the chain

Front 78

Poly saturated chains

Back 78

Have many double covalent bonds

Front 79

Fats

Back 79

Made up of two molecules, glycerol and fatty acid chains.

Fatty acid chains bound to a glycerol group buy a dehydration synthesis reaction which forms an ester linkage. The carboxyl group of the acid reacts with the hydroxyl group of the glycerol molecule

Front 80

Triglycerides

Back 80

Three fatty acid chains linked to a glycerol group. Primarily energy source

Front 81

Saturated fat

Back 81

Lipid composed of unsaturated fatty acids with single Bonds in their hydrocarbon chain

Front 82

Unsaturated fat

Back 82

Lipid composed of unsaturated fatty acids with double Bonds in their hydrocarbon chain

Front 83

Phospholipid

Back 83

Lipid with two fatty acids and a phosphate group bonded to a glycerol group. Primary lipids in cell membranes. Hydrophobic and philic

Front 84

Structure of phospholipids

Back 84

The phosphate portion or head region is polar and hydrophilic. Fatty acid chains are nonpolar and hydrophobic. They make a bilayer cell membrane

Front 85

Amino acids

Back 85

A molecule that has a carboxyl group and an amino group. Serves as the monomer subunit of proteins

Front 86

Amino acids

Back 86

A molecule that has a carboxyl group and an amino group. Serves as the monomer subunit of proteins

Front 87

What makes up an amino acid

Back 87

Central carbon with a carboxyl group and an amino group attached at each end. The central carbon also has a radical group which leads to variation between Amino acids

Front 88

How many types of amino acids are

Back 88

There are 20 kinds. 8 are essential and 12 are not

Front 89

Protein

Back 89

Large molecule with many amino acid subunits that are joined by peptide bonds folded into a specific 3D shape

Front 90

What do proteins do

Back 90

They carry vital structural and functional roles. Also hormones, carry substances across membranes, recognition and receptor protein, on cell membranes, enzymes, antibodies

Front 91

Peptide bonds

Back 91

Covalent bond that links amino acids

Front 92

Peptide

Back 92

Chain of amino acids subunits connected by peptide bonds

Front 93

Polypeptide

Back 93

Peptide with more than 50 amino acids

Front 94

Are proteins polymers

Back 94

Yes they're made up of monomers amino acids subunits

Front 95

How are amino acids bonded

Back 95

Covalent bonds by dehydration

Front 96

What is the process of amino acid bonding

Back 96

The amino group, nh2, I want amino acid, in terminal, will form a bond with a carboxyl group, C terminal cooh -, of another amino acid

Front 97

Denaturation

Back 97

The loss of the structure and function of a protein. Can be caused by temperature and pH changes.

The protein is in active if the structure is changed and permanent if the bonds are broken

Front 98

Nucleic acid function

Back 98

Responsible for the synthesis of proteins. Also can transport chemical potential energy

Front 99

DNA

Back 99

Stores genetic information and is found in the nucleus

Front 100

RNA

Back 100

Communicates to the ribosome to produce a specific protein and is found in the nucleus and cytoplasm

Front 101

What molecules can transport chemical potential energy

Back 101

Adenine triphosphate and guanosine triphosphate. There is also a m p, NAD, and f a d

Front 102

Nucleotide

Back 102

The building block of nucleic acid. Consists of a 5 carbon sugar and nitrogenous base and one to three phosphate groups

Front 103

Nucleotides are grouped into

Back 103

Purines which are double rings and pyrimidines which are single ring

Front 104

Purines

Back 104

Adenine and guanine

Front 105

Pyrimidines

Back 105

Thymine cytosine and uracil

Front 106

Structure of DNA and RNA

Back 106

Poly nucleotide chains were a phosphate group is bonded to the 5 carbon of one sugar group in history carbon of another sugar group

Front 107

Phosphodiester Bond

Back 107

It's a link formed between nucleotides by a phosphate Bridge

Front 108

DNA structure

Back 108

Strands are in opposite directions and they're held together by hydrogen bonds between the nitrogenous base pairs.

Front 109

Atom can form how many hydrogen

Back 109

Two hydrogen bonds

Front 110

How many hydrogen bonds can guanine form

Back 110

3

Front 111

How do enzymes speed up a chemical reaction

Back 111

Enzyme lowers the activation energy required to break chemical bonds

Front 112

Enzyme

Back 112

Biological catalyst, usually A protein that speeds up a chemical reaction

Front 113

Substrate

Back 113

The substance that is recognized by and binds to an enzyme

Front 114

Active sites

Back 114

A pocket or Groove in an enzyme that binds its substrate

Front 115

Induced fit model

Back 115

A model of enzyme activity that describes how an enzyme changes shape to better accommodate a substrate. Enzymes temporarily attached to the substrate allow the reaction and then is released so it can happen again

Front 116

Induced fit model long description

Back 116

Enzymes only interact with the substrate at their active site. The groove is specific to the shape of the substrate. This model explains enzyme-substrate reaction. This stresses the bonds of the substrates enzyme substrate complex so the reaction occurs less energy. The transition state is when stuff happens

Front 117

Competitive inhibition

Back 117

When something blocks the enzyme activity

Front 118

Noncompetitive inhibition

Back 118

When something binds to the enzyme somewhere where it's not the active site but it changes the shape