Chapter 3-6

Question 1

Hydrophobic vs hydrophilic

Answer 1

Hydrophobic: water fearing(lots of non polar, covalent bonds)

Hydrophilic: water loving(polar or ionic bonds, a charge)

Question 2

Monomers vs Polymers

Answer 2

Monomer: molecular subunit used to build a macromolecule; “one part”; One link in a chain

Polymerize through condensation reactions/dehydration reactions: new bond results in loss of water molecule, GROWS POLYMERS

Polymer: structure of large unit of monomers that are bonded together

Polymerization: process of linking monomers together

Question 3

4 main classes of macromolecules

Answer 3

proteins, lipids, carbohydrates, and nucleic acids

Question 4

Carbohydrate(monosaccharide)

Answer 4

large molecule: polysaccahride

function: energy storage, receptors, structure of plant cell wall

To identify: C, H, and O; Oh’s on all carbons except one

Question 5

Monosaccharides in Carbohydrates

Answer 5

Monosaccharides(simple sugars) are their monomers

Di – two monosaccharides; Oligo – “few” oligosaccharide; Poly – “many” - polymers

Question 6

Examples of monomers in carbohydrates

Answer 6

Monomers can vary their structure, slight changes can create big changes in polymers

5-carbon sugars:
Deoxyribose does not completely conform(DEOXY); Missing an oxygen(4 oxygen and 5 hydrogen)

Ribose includes five oxygen and hydrogen

Question 7

3 carbon sugar of carbohydrates

Answer 7

glyceraldehyde(VIEW NOTE IMAGES)

Question 8

6 carbon sugars

Answer 8

VIEW NOTE IMAGES

glucose, fructose, calactose; C/6 H/12 O/6

Carbon and oxygen the same in glucose, double the amount of hydrogen

Fructose and Galactose includes the same amount of atoms as glucose, but arranged differently for different reactions

Question 9

Polymers of Glucose

Answer 9

VIEW NOTE IMAGES
Alpha linkages: branched chains for energy storage

Beta linkages: straight chains for structure

Recognize that all these monomers are similar In structure, and vastly changed by shifting around functional group location

Question 10

Polysaccharide of Carbohydrates uses

Answer 10

Variation in formation

Can be used to store chemical energy in plant cells(STARCH)

Provide structural support to insect and fungi exoskeletons(CHITIN)

Glycogen: energy storage

Cellulose: plant cell walls

MODFIFIED POLYSACCHARIDE: peptidoglycan

Question 11

IMAGES OF CarBOHYDRATES IMPORTANT

Answer 11

REVIEW ON PAGE 12

Question 12

Nucleic Acids(nucelotide)

Answer 12

large molecule: nucleic acid

function: informational storage and transfer

To identify: contain N in rings,nucleotides made of sugar(ribose, RNA or deoxyribose, DNA), phosphate and nitrogenous base

Question 13

ATP nucleotide

Answer 13

Adenosine Triphosphate
ATP = energy

Question 14

Sugar/Phosphate backbones and nitrogenous bases of nucleic acids

Answer 14

Sugar = ribose(RNA or deoxyribose) DNA; Phosphate group; Nitrogenous bases

Finding 3’ and 5’ prime ends are important! It determines where things go/attach when making RNA and DNA(PAGE 20); (1’ holds nitrogenous base, 3’ is end of structure and 3’ & 5’ brought together by phosphate group specifically attached to the 5’)

Molecule of RNA and DNA, based on some characteristics

Types of nitrogenous bases hanging off carbons

3’ and 5’ carbons joined by phosphate

Question 15

DNA: genetic footprint

Answer 15

Just means information to create organisms…

Double stranded macromolecule held together by hydrogen bonds; Adenine and thymine are always a pair; Guanine and Cytosine are always a pair

If base pairs mismatched, hydrogen bonds will not line up correctly

Hydrogen bonds individually are weak, but stronger in large numbers(like in DNA!)

In double stranded DNA, backbones must run in antiparallel directions!

Example: two cars on a two lane road going, imagine headlights going opposite directions

5’ and 3’ are on opposite ends

Question 16

RNA

Answer 16

link between DNA(blueprint) and protein(does the work)
o mRNA, tRNA, rRNA, and more!

Question 17

DNA AND RNA IMAGES

Answer 17

PGS 20-23

Notice structures of nucelotides, RNA AND DNA, and the base pairs to recognize them

Question 18

Protein(Amino acid)

Answer 18

large molecule: polypeptide or protein

function: enzymes, structure, receptors, transport, and more

To identify: contain N, have N-C-C backbone

Question 19

Protein(Amino acid)

Answer 19

large molecule: polypeptide or protein (Peptide/oligopeptide/polypeptide are mostly synonyms for proteins)

function: enzymes, structure, receptors, transport, motion, regulation

To identify: contain N, have N-C-C backbone

Mostly CHON and some S

Question 20

Protein formation

Answer 20

Proteins = amino acids joined by peptide bonds

form by dehydration synthesis(take out 2 H and 1 O to take water out, H2O)

Question 21

R groups of Proteins

Answer 21

Electrically charged side chains: (Acidic groups add protons to group; Basic groups); both groups are hydrophilic; charges die chains can form ionic and hydrogen bonds

Polar side chains: Unequal tug of electrons on two end groups; Hydrophilic; OH, hydroxyl group

Nonpolar side chains; Do NOT interact with water(hydrophobic); To identify, look for methyl groups, ring structures, CH2, CH3, rings(order different but are same thing)

Question 22

C- terminus/ N-terminus of proteins

Answer 22

C: Carboxyl group

N: Amino group

IMAGE ON PAGE 19

Question 23

What are the levels of protein structure and how is protein structure determined?

Answer 23

primary, secondary, tertiary, and quaternary

Question 24

Protein Structure

Answer 24

Primary: specific amino acid sequence(see image on page 23)

Secondary: folding of amino acid chains

Tertiary: final folded shape of globular protein; all secondary structures complete protein folding

Quaternary: when two or more chains(subunits) associate with each other
o Example: hemoglobin
o Multiple complete proteins can be “subunits” of an even larger protein complex

VISUALIZATION ON PAGE 24 HELPS!!!!!!!!

Question 25

What sorts of things can chage in protein structure?

Answer 25

Secondary structures: Amino acid polymers(proteins) can flex and bend; They form the most diverse set of shapes for organic molecules

Chaperone proteins: Folding

Unfolding proteins: Ribonuclease protein folded to ribonuclease protein denatured(unfolded); The secondary and tertiary structures change in the process; Only thing that remains the same is primary structures

Changes
* Mechanically(bumping into things)
* Thermal(temperature changes)
* Chemical(pH level dependent, ion concentration dependent)

Question 26

Proteins; prion infectivity is linked to structure

Answer 26

Forcing other proteins to take on incorrect shapes to cause infection and killing of cells/brain cells is quite dangerous!

IMAGE ON PAGE 25

Question 27

Lipids(are not polymers)

Answer 27

(glycerol, fatty acids joined)

large molecule: fats, oils, waxes, phospholipids, steroids

function: membrane structure, energy storage, insulation

to identify:

Question 28

saturated fats

Answer 28

no double bonds between carbons fo the fatty acids; More dense/packed in pretty tightly

Question 29

Unsaturated fats

Answer 29

at least one double bond; Form kinks(When kinked, can’t pack in tightly); Fluid at room temp.

Question 30

Cis vs. Trans Fats

Answer 30

Trans fat: not normally found in food supply; Rotated around the double bond; Enzymes don’t break these down, they don’t go away

Helped at first so food could sit for long periods of time; but not good for the body(molds and bacteria cannot break it down, so your body cannot really do it either); 8 to 30 times increased risk of heart disease

Cis fatty acid: Seen more inn sections; Both sides have tail pointing downward, normal