CH5: THE STRUCTURE AND FUNCTION OF LARGE BIOLOGICAL MOLECULES

Question 1

large, complex molecules - carbs, protein, nucleic acids

have unique emergent properties from orderly arrangement of atoms

Answer 1

macromolecules

Question 2

what are the 4 large molecules of life

Answer 2

carbohydrates, lipids, proteins, nucleic acids

Question 3

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

Answer 3

polymer

Question 4

the smaller, repeating molecules that are the building blocks of a polymer

Answer 4

monomers

Question 5

what are the 3 macromolecules

Answer 5

carbs (polymers of sugar and starches)
proteins (polymers of amino acids)
nucleic acids (polymers of nucleotides (DNA, RNA)

Question 6

specialized macromolecules that speed up chemical reactions such as those that make or break down polymers

usually proteins that ends in ASE

Answer 6

enzymes

Question 7

reactions in which two monomers are covalently bonded to each other through the loss of a water molecule

short polymer + unlinked monomer - water = longer polymer

Answer 7

dehydration reactions

Question 8

reverse of the dehydration reaction

disassemble polymers into monomers

longer polymer + water = break bond

Answer 8

hydrolysis

Question 9

includes sugars and polymers of sugars

Answer 9

carbohydrates

Question 10

simple sugars/carbs

usually have CH2O (i.e. glucose, the most common)

classified by location of carbonyl group and number of carbons in carbon skeleton

Answer 10

monosaccharides

Question 11

double sugars, two monosaccharides joined by a glycosidic linkage

Answer 11

disaccharides

Question 12

a covalent bond formed between two monosaccharides by a dehydration reaction (remove water makes a link to combine 2 sugars)

Answer 12

glycosidic linkage

Question 13

macromolecules, polymers with a few hundred to a few thousand monosaccharides joined by glycosidic linkages

composed of at least two sugar building blocks

polymers of sugars, have energy storage and structural roles

Answer 13

polysaccharides

Question 14

a polymer of only glucose monomers stored by plants

store surplus starch as granules within chloroplasts and other plastids

UNBRANCHED/SOMEWHAT UNBRANCHED

Answer 14

starch

Question 15

simplest form of starch

Answer 15

amylose

Question 16

a polymer of glucose that is amylopectin but HIGHLY BRANCHED; stored by animals

Answer 16

glycogen

Question 17

polymer of glucose with differing glycosidic linkages in the 2 polymers major component of the tough walls that enclose plant cells

MOST ABUNDANT ORGANIC COMPOUND

UNBRANCHED (straight, unflexible)

difference based on two rings for glucose - alpha and beta

Answer 17

cellulose

Question 18

enzymes that digest starch by hydrolyzing ______ linkages can’t hydrolyze _____ linkages in cellulose

Answer 18

alpha, beta

Question 19

structural polysaccharide found in animals

builds exoskeletons in arthropods

provides structural support for the cell walls of fungi

used in surgical thread

cicada/locusts leave it behind when hatch

Answer 19

chitin (pronounced kaitin)

Question 20

mix poorly, if at all with water

NOT POLYMERS (not repeated structures); too small to be macromolecules

mostly hydrocarbon regions (form nonpolar covalent)

Answer 20

lipids

Question 21

constructed from two kinds of smaller molecules - glycerol and fatty acids

Answer 21

fat

Question 22

long carbon skeleton, usually 16-18 carbon atoms in length

Answer 22

fatty acid

Question 23

three-carbon alcohol with a hydroxyl group attached to each carbon

Answer 23

glycerol

Question 24

three fatty acids linked to one glycerol molecule

most potential energy

Answer 24

triacylglycerol

Question 25

NO DOUBLE BONDS between carbon atoms said to be _______ with oxygen most animal fats: butter, lard, etc that are solid at room temp

Answer 25

saturated fatty acid

Question 26

how do saturated fats contribute to cardiovascular diseases?

Answer 26

through plaque deposits

Question 27

unsaturated fats with trans double bonds when hydrogenating vegetable oils

Answer 27

trans fats

Question 28

converts unsaturated to saturated by adding hydrogen

Answer 28

hydrogenation

Question 29

HAS DOUBLE BONDS with fewer H atoms on each double bond safer than saturated most plant and fish fats - olive oil, etc; liquid at room temp

Answer 29

unsaturated fatty acid

Question 30

what is the main functions of fat?

Answer 30

long term storage of energy; cushion organs and be insulative

Question 31

similar to a fat molecule but has only two fatty acids attached to glycerol rather than three hydrophilic, phosphate containing head hydrophobic tail (1 tail with kink from double bond) self assemble without energy needed

Answer 31

phospholipid

Question 32

lipids characterized by a carbon skeleton consisting of four fused rings

Answer 32

steroids

Question 33

a type of steroid that is crucial in animals and a precursor from which other steroids are synthesized high level is highly hydrophobic and bad for health

Answer 33

cholesterol

Question 34

account for 50% dry mass of most cells functions: defense, energy storage, transport across and out cell, cellular communication, movement, structural support (very versatile)

Answer 34

protein

Question 35

selective acceleration of chem rxns - changes chem rxn rate without itself being changed into a different thing in the process

Answer 35

enzymatic proteins

Question 36

protection against disease - makes antibodies that bond to invaders

Answer 36

defensive proteins

Question 37

storage of amino acids

Answer 37

storage proteins

Question 38

moves substances (i.e. channel proteins in cell membrane)

Answer 38

transport proteins

Question 39

coordination of organism's activities signal proteins that bring something to tell the cell what to do (triggers a series of things for the cell to do) i.e. insulin to regulate sugar

Answer 39

hormonal proteins

Question 40

response of cell to chemical stimuli - bind to signal molecules to transmit second messengers to trigger something else

Answer 40

receptor proteins

Question 41

movement - truckers of the cell that transport from one side to the other of a cell or out of it i.e. striated muscle - actin and myosin (release grab pull to shorten muscle)

Answer 41

contractile and motor proteins

Question 42

support; polypeptide braided rope; i.e. keratin in hair

Answer 42

structural protein

Question 43

chemical agents that selectively speed up chemical reactions without being consumed by the reactions brings 2 things close; protein changes shape and jams two together; can do things without getting used up

Answer 43

catalysts

Question 44

a polymer of amino acids; unbranched polymers built from amino acids

Answer 44

polypeptide

Question 45

the covalent bond that joins amino groups to each other through a dehydration reactions

Answer 45

peptide bond

Question 46

a biologically functional molecule made up of one or more polypeptides, each folded and coiled into a specific 3D structure

Answer 46

protein

Question 47

an organic molecule with both an AMINO group and CARBOXYL group; 20 types

Answer 47

amino acid

Question 48

t/f: polypeptides vary in length from few to 1K+ monomers

Answer 48

TRUE

Question 49

carboxyl end of polypeptide

Answer 49

C-terminus

Question 50

amino end of polypeptide

Answer 50

N-terminus

Question 51

a protein's sequence of amino acids (from amino to carboxyl end) determined by inherited genetic info

Answer 51

1* Primary Structure

Question 52

the coiled and folded structure that results from H-bonds between repeating constituents of the polypeptide backbone H-bonds between backbone in diff sections of polypeptide forms 2 shapes - coiled alpha helix or folded beat pleated sheet

Answer 52

Secondary Structure 2*

Question 53

a delicate coil held together by H-bonding between every 4th amino acid

Answer 53

alpha helix

Question 54

folded/bended structure; long sheet

Answer 54

beta pleated sheet

Question 55

the overall shape of a polypeptide resulting from interactions from the side chains (R-groups) of the various amino acids more bending, folding, twisting by H-bonds, ionic bonds, hydrophobic interactions, van der waals

Answer 55

Tertiary Structure 3*

Question 56

contributes to the tertiary structure; _________ parts want to stay in and hydrophilic wants to stay out

Answer 56

hydrophobic interaction

Question 57

really strong covalent bonds that may further reinforce that protein shape only those with sulfur in their amino acid - Methionine & Cysteine

Answer 57

disulfide bridges

Question 58

the overall protein structure that results from the aggregation of these polypeptide subunits 2 or more proteins that have to come together and act as 1 to do something i.e. collagen, hemoglobin

Answer 58

Quaternary Structure 4*

Question 59

an inherited blood disorder caused by the substitution of one amino acid (valine) for the normal one (glutamic acid) at a particular position in the beta unit primary structure of hemoglobin, the protein that carries oxygen in red blood cells shape doesn't do stuff efficiently makes you less susceptible to malaria

Answer 59

sickle-cell disease

Question 60

the change caused by an altered environment that leads to the weak chemical bonds and interactions within a protein may be destroyed; the loss of a proteins native structures affects physical and chemical conditions alterations in pH, salt conc, temp, etc can unravel protein ______ protein = biologically inactive

Answer 60

denaturation

Question 61

used to determine the 3D structure of many proteins

Answer 61

X-ray crystallography

Question 62

other protein molecules that assist the proper folding of other proteins

Answer 62

Chaperonins