Ap Bio Midterm - Chapter 5

Front 1

Large molecules made up of repeating molecules

Back 1

Polymers

Front 2

Subunits of Polymers - linked together by dehydration synthesis, requiring ATP and enzymes; separated by hyrdolysis

Back 2

Monomers

Front 3

Monomers connected by a reaction in which two molecules are covalently bonded to each other through the loss of a water molecule

Back 3

Condensation reaction (dehydration synthesis)

Front 4

Bonds between monomers are broken by the addition of water molecules

Back 4

Hydrolysis

Front 5

Polysaccharides - startch, glycogen, cellulose, chitin

Back 5

Carbohydrates

Front 6

Simple surgars, monomers of Carbohydrates

Back 6

Monosacchardies

Front 7

Two monosacchardies joined by glycosidic linkage

Back 7

Disacchardies

Front 8

Covalent bond formed between two monosaccharides by dehydration synthesis

Back 8

Glycosidic Linkage

Front 9

Many monosaccharides joined by glycosidic linkage

Back 9

Polysaccharides

Front 10

Storage polysaccharide - polymer consisting entirely of glucose monomers - joined by 1-4 linkages

Back 10

Starch

Front 11

Polymer of glucose that are stored in liver and muscle cells

Back 11

Glycogen

Front 12

Major component of tough walls that enclose plant cells

Back 12

Cellulose

Front 13

Used by anthropods to build their exoskeleton - becomes hardened when encrusted with CaCO4

Back 13

Chitin

Front 14

Little or no affinity for water; does not include polymers - behavior based on their molecular structure - mostly of hydrocarbons (nonpolar)

Back 14

Lipids

Front 15

Constructed by glycerol and fatty acids (using dehydration synthesis - creates bond ester linkage; no monomers)

Back 15

Fats

Front 16

Alcohol with three carbons, each with a hydroxyl group

Back 16

Glycerol

Front 17

Long carbon skeleton - one end with carboxyl group; chain of nonpolar C-H bonds

Back 17

Fatty acids

Front 18

Three fatty acids (tails), linked to one glycerol molecule (the head)

Back 18

Triaclyglycerol

Front 19

No double bonds between the carbon atoms; saturated with hydrogen - solid at room temperature

Back 19

Saturated Fatty Acid

Front 20

One or more double bonds - kink in tail wherever a double bond occurs - liquid

Back 20

Unsaturated fatty acid

Front 21

Only two fatty acid tails - third joined to a phosphate group - negative in electron charge - tails are hydrophobic

Back 21

Phospholipids

Front 22

Lipids characterized by a carbon skeleton consisting of four fused rings

Back 22

Steroids

Front 23

Animal cell membranes; precursor from which other steroids are synthesized - control fluidity of cell membrane

Back 23

Cholesterol

Front 24

One or more polypeptides folded and coiled to specific conformations - function depends on its structure

Back 24

Protein

Front 25

Organic molecules possessing both carboxyl and amino groups - alpha carbon with an amino group, carboxyl group, a hydrogen atom, and a variable group (R)

Back 25

Amino acids

Front 26

Physical and chemical properties that determine the unique characteristics of an amino acid

Back 26

R group (side chain)

Front 27

Result of when two amino acids have both carboxyl group adjacent with other amino group

Back 27

Peptide bond

Front 28

Unique sequence of amino acids - can affect a protein's conformation

Back 28

Primary structure

Front 29

Coiled or folded patterns - result of hydrogen bonds at intervals along the polypeptide backbone

Back 29

Secondary structure

Front 30

Coil held together by hydrogen bonding between every fourth amino acid

Back 30

Alpha helix

Front 31

Two or more regions of the polypeptide chain lie parallel each other - hydrogen bonds hold the structure together - usually in fibrous proteins

Back 31

Beta pleated sheets

Front 32

Superimposed on the patterns of secondary structure - irregular contortions from interactions between side chains (R groups) of the various amino acids

Back 32

Tertiary structure

Front 33

Weak chemical bond formed when molecules that do not mix with water coalesce to exclude the water

Back 33

Hydrophobic interaction

Front 34

Covalent bonds form where two cyteine monomers (amino acids with sulfhydryl groups, -SH on their side chains), are brought close together by the folding of the protein (-S-S-)

Back 34

Disulfide bridges

Front 35

Overall protein structure that results from the aggregation of the two or more polypeptide chains

Back 35

Quaternary Structure

Front 36

Unravelling of the protein - inactive

Back 36

Denaturation

Front 37

Monomers with nucleic acids as polymers - nitrogeneous base, pentose (5-carbon sugar), and phosphate group

Back 37

Nucleotides

Front 38

6-membered ring of carbon and nitrogen atoms - Cytosine (C), Thymine (T), and Uracil (U) - 1 ring

Back 38

Pyrimidine

Front 39

6-membered ring fused to a 5-member ring - Adenine (A), and Guanine (G) - 2 rings

Back 39

Purines

Front 40

Pentose connected to the nitrogeneous base in DNA

Back 40

Deoxyribose

Front 41

Pentose connected to the nitrogeneous base in RNA

Back 41

Ribose

Front 42

Nucleic acid polymer - nucleoties joined by covalent phosphodiester linkages between the phosphate of one nucleotide and the sugar of the next

Back 42

Polynucleotide

Front 43

2 polynucleotides that spiral around

Back 43

Double helix