Biology Ch. 5

Front 1

polymer

Back 1

long molecule consisting of many identical or similar building blocks linked by covalent bonds

Front 2

monomers

Back 2

the repeating units that serve as the building blocks of a polymer

Front 3

condensation reaction; dehydration reaction

Back 3

a reaction in which two molecules become covalently bonded to each other throught the loss of a small molecule, usually water

Front 4

hydrolysis

Back 4

a chemical process that lyses or splits molecules by the addition of water; an essential process in digestion

Front 5

carbohydrate

Back 5

includes both sugars and their polymers

Front 6

monosaccharides

Back 6

the simplest carbohydrates which are known as simple sugars

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disaccharide

Back 7

consists of two monosaccharides

Front 8

glycosidic linkage

Back 8

a covalent bond formed between two monosaccharides by a dehydration reaction

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polysaccharides

Back 9

macromolecule (polymers with a few hundred to thousand monosaccharides joined by glycosidic linkage

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starch

Back 10

a storage polysaccharide of plants

Front 11

glycogen

Back 11

a polymer of glucose that is like amylopectin but more extensively branched; animals store this polysaccharide

Front 12

cellulose

Back 12

a major component of the tought walls that enclose plant cells

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chitin

Back 13

the carbohydrate used by arthopods (insects, spiders, crustaceans, and related animals) to build their exoskeletons

Front 14

exoskeleton

Back 14

a hard case that surrounds the soft parts of the animal

Front 15

lipid

Back 15

one of a fammily of compounds, including fats, phospholipids, steroids, that are insoluble in water

Front 16

fat (triacylglycerol)

Back 16

a biological compound consisting of 3 fatty acids linked to one glycerol molecule

Front 17

fatty acid

Back 17

a long carbon chain carboxylic acid. these vary in length and location of double bonds. 3 of these linked to a glycerol molecule form fat

Front 18

saturated fatty acid

Back 18

there are no double bounds between the carbon atoms composing the tail, and as many hydrogen atoms as possible are bounded to the carbon skeleton.

Front 19

unsaturated fatty acid

Back 19

has one or more double bonds, formed by the removal of hydrogen atoms from the carbon skeleton; the fatty acid will have a kink in its shape wherever a double bond occurs

Front 20

phospholipids

Back 20

molecules that constitute the inner bilayer of boiological membranes, having a polar, hydrophilic head and a nonpolar, hydrophobic tail

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steroids

Back 21

a class of lipids characterized by a carbon skeleton consisting of four rings with various functional groups attached

Front 22

cholesterol

Back 22

a steroid which is a common component of animal cell membranes and is also the precursor from which other steroids are synthesized

Front 23

protein

Back 23

a 3-D biological polymer constructed from a set of 20 different monomers called amino acids

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polypeptides

Back 24

polymers of aminoacids

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amino acids

Back 25

organic molecules possessing both carboxyl and amino groups

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peptide bond

Back 26

the covalent bond between two amino acid units, formed by condensation synthesis

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primary structure

Back 27

the level of protein structure referring to the specific sequence of amino acids

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secondary structure

Back 28

the localized, repetitive coiling or folding of the polypeptide bacbone of a protein due to hydrogen bond formation between peptide linkages

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alpha helix

Back 29

a spiral shape constituting one form of the secondary structure of proteins arising from a specific hydrogen-bonding structure

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pleated sheet

Back 30

one form of the secondary structure of proteins in which the polypeptide chain folds back and forth, or where two regions of the chain lie parallel to each other and are held together by hydrogen bonds

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tertiary structure

Back 31

irregular contortions of a protein molecule due to interactions of side chains involved in hydrophobic interactions, ionic bonds, hydrogen bonds, and disulfide bridges

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hydrophobic interaction

Back 32

a type of weak chemical bond formed when molecules that do no mix with water coalesce to exclude the water

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disulfide bridges

Back 33

strong covalent bonds between two cysteine monomers (amino acids with sulfhydryl groups on their side chains)

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quaternary structure

Back 34

the particular shape of a complex, aggregate protein, defined by the characteristic 3-D arrangement of its constituent subunits, each a polypeptide

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denaturation

Back 35

for proteins a process in which a protein unravels and loses its native conformation, thereby becoming biologically inactive. denaturation occurs under extreme conditions of pH, salt concentration, and temperature

Front 36

chaperone proteins

Back 36

molecules that function as temporary braces in assisting the folding of other proteins