Chapter Three

Question 1

Structural isomers?

Answer 1

atoms are joined together differently, but same chemical composition

Question 2

cis‐trans isomers?

Answer 2

different orientation around a double bond

Question 3

Optical isomers?

Answer 3

occur when C atom has four different groups
attached to it
this makes it an asymmetric carbon / mirror image

Question 4

Macromolecule?

Answer 4

polymer containing thousands or more atoms

Question 5

describe the hydroxyl group

Answer 5

polar charged functional group -OH that help water dissolve molecules by forming hydrogen bonds with water often helps condensation reactions do its thing

Question 6

describe the Carboxyl functional group

Answer 6

COOH
charged acidic, because it gives away a H+. Enters into condensation reaction by giving up an OH, and can be important in energy releasing reactions and is soluble in water

Question 7

Describe the Amino group

Answer 7

NH2
charged basic because it accepts H+ and forms NH3* and enters into condensation by giving up H+ Water soluble and is considered a weak base

Question 8

describe phosphate group

Answer 8

PO4
charged, acidic, because it gives up a H+ water soluble, and important in energy transfer
enters into condensation reaction by giving up OH when bonded to another phosphate

Question 9

What are the four macromolecules?

Answer 9

Proteins
Carbohydrates
Lipids
Nucleic Acids

Question 10

What are the building blocks of macromolecules?

Answer 10

All except lipids have MONOMERS that create polymers

and macromolecules are polymers that have thousands of atoms

building blocks of macromolecules are monomers

Question 11

What is a polypeptide chain?

Answer 11

single, continuous chain of protein monomers, amino acids joined by covalent bonds

Question 12

Describe the structure of an amino acid.

Answer 12

Central carbon with an amino group on one side, carboxyl group on the other

R group (side chain) (variable part) on top, and a hydrogen below the Carbon

Question 13

How do you group amino acids?

Answer 13

side chains (R-groups)
they have certain properties that place them in their groups
There are 20 different amino acids

Question 14

What is primary structure?

Answer 14

the basic sequence (chain) of amino acids (monomers)
this determines the other structures
composed of covalent bonds

Question 15

what is secondary structure?

Answer 15

repeated spacial patterns in different regions of a poly peptide chain that is composed of H bonds

coils and sheets of the primary structure

Question 16

What are the two types of secondary structure?

Answer 16

Alpha helix- right handed coil that results from H bonding between (N-H) and (C=O)

Beta pleated sheets- when two or more chains align and H-bonds form between (N-H) and (C=O)

Question 17

what is tertiary structure

Answer 17

the folding that results in the 3D shape of one polypeptide

it is determined by interactions between R groups, which form disulfide bonds, hydrogen bonds etc.

Question 18

what is quaternary structure?

Answer 18

the overall protein shape due to the interactions of multiple polypeptides chains that make up the protein

Question 19

What is a denatured protein?

Answer 19

a protein that’s secondary and tertiary structure and quaternary structure has broken down

Question 20

Why is a proteins primary sequence not broken down during denaturation?

Answer 20

because primary structure is made of peptide bonds which are covalently bonded which is very difficult to break

Question 21

What is the process that breaks down primary structure?

Answer 21

hydrolysis (adding water breaks the covalently bonded monomers up)

Question 22

What affects secondary and tertiary denaturation?

Answer 22

High temperature, pH changes, high concentrations of polar molecules, and non polar substances

Question 23

How do proteins interact with other molecules?

Answer 23

They bind non-covalently with specific molecules.

Whether or not a protein can bind with another molecule depends on the
1. shape
2. chemistry of its side chains

If it successfully bonds, it can change the proteins shape

Question 24

state general formula of a carbohydrate

Answer 24

(C1H2O1)n

Question 25

why are carbohydrates so important to life?

Answer 25

1. they act as sources of stored energy 2. they act as transporters of energy 3. they act as carbon skeletons for other molecules 4. they form extracellular structures (cell wall)

Question 26

Monosaccharides?

Answer 26

simplest sugars Eg. glyceraldehyde-3C, Ribose-deoxyribose-5C, Glucose, Mannose, Fructose-6C Can be in straight chain or ring form

Question 27

Disaccharides?

Answer 27

two simple sugars linked by *covalent* bonds Eg. sucrose, or Lactose Sucrose = glucose + fructose Lactose = glucose + galactose

Question 28

Oligosaccharides?

Answer 28

3-20 monosaccharides oligo meaning (a few) Eg. human breast milk

Question 29

Polysaccharides?

Answer 29

hundreds or thousands of monosaccharides Eg. cellulose, starch glycogen

Question 30

What is the bond that joins monosaccharides?

Answer 30

glycosidic linkage which is a covalent bond through a condensation reaction

Question 31

What disaccharide is created by linking two beta D glucose by 1st C and 4th C?

Answer 31

Cellobiose is formed by glycosidic linkage.

Question 32

Three types of polysaccharides?

Answer 32

Cellulose - very stable good for structural component *unbranched* (tightly packed, linearly Starch - glucose storage in plants *branched* (limits the amount of h-bonds that can form, less compact Glycogen - glucose storage in animals *highly branched* makes it more compact than starch

Question 33

What are lipids? What keeps them together?

Answer 33

*nonpolar* hydrocarbons that are insoluble in water *weak vanderwaals forces are what keep it together

Question 34

why do lipids not have monomers?

Answer 34

because the molecules of lipids *hydrocarbons* don't bond covalently molecules of lipids are not glycerol, fatty acids and phosphate, they are simply the C's H's

Question 35

Explain the types of lipids

Answer 35

1. fatty acids - non polar hydrocarbon chain with a polar *carboxyl* group 2. triglycerides - are three fatty acids plus a glycerol 3. phospholipids - are fatty acids bound to a glycerol but a phosphate group replaces one fatty acid

Question 36

how are glycerol and fatty acids joined?

Answer 36

When the carboxyl of the fatty acids and hydroxyl of glycerol in an *ester linkage* which is a covalent bond and it releases three water molecules

Question 37

How are triglycerides broken down?

Answer 37

Hydrolysis of triglycerides happen when three molecules of water are added

Question 38

Saturated fatty acid and unsaturated fatty acids.

Answer 38

Saturated fatty acids are when there are no double bonds between carbons *saturated with hydrogen atoms, tightly packed* usually appear as solids at room temp Unsaturated fatty acids are when one or more double bonds appear in a hydrocarbon chain, *the double bond kinks prevent close packing usually appear as liquids at room temp

Question 39

Molecules bearing both polar and non-polar groups are said to be?

Answer 39

amphipathic

Question 40

What is the point of lipids?

Answer 40

1. they provide nutrients for organisms 2.*store carbon and energy* 3. play structural roles in membranes 4. function as hormones 5. thermal insualtion

Question 41

what is a chaperone and why are they important?

Answer 41

Chaperone proteins, or molecular chaperones, are proteins that assist others to fold properly during or after synthesis or to refold after partial denaturation If a protein becomes denatured, the chaperone proteins are useful

Question 42

what are organic compounds made of?

Answer 42

They are made of monomers except lipids and the elements that make them up are Carbon, Hydrogen, Nitrogen, and and Oxygen

Question 43

what are the function/ importance of proteins?

Answer 43

THEY DO MOST OF THE WORK! 1. Enzymes proteins - they catalyze/speed up reactions 2. structural - provide physical stability and movement 3. defensive proteins -recognize and respond to non self substances 4. signaling proteins - control physiological process (hormones) 5. receptor proteins - receive and respond to chemical signals 6. membrane transporters - regulate the membrane 7. storage proteins - store amino acids 8. transport proteins - bind and carry substances in the cell 9. gene regulation - determine the rate of expression of a gene 10. motor proteins - cause movement of structures in the cell