Biomolecules

Question 1

Adhesion

Answer 1

“sticks” to other substances

Question 2

Cohesion

Answer 2

“sticks” to itself

Question 3

Surface tension is due to

Answer 3

cohesion of H2O cules to one another and adhesion of H2O to the surface

Question 4

hydrophobic

Answer 4

repels water

Question 5

hydrophilic

Answer 5

attracts water

Question 6

condensation reaction

Answer 6

reaction in which H2O is produced

Question 7

hydrolysis reaction

Answer 7

reaction in which H2O is consumed (reverse of condensation); this is how we digest food, and also why we need to consume a lot of water.

Question 8

transpiration

Answer 8

how H2O moves through plants using adhesion to bring the water up the stem and to the top of the plant

Question 9

Some important properties of H2O

Answer 9

• Less dense as a solid
• Temperature buffer (changes temp slowly and absorbs a lot of nrg)
• can undergo H2O dissociation

Question 10

H2O dissociation

Answer 10

H2O is pulled apart in the reaction 2H20 -> H3O + OH

This occurs once in every 10^7 cules

Question 11

functional groups

Answer 11

groups added to carbon-based molecules that give it its special properties

Question 12

polymer

Answer 12

chain of biomolecules

Question 13

monomers

Answer 13

one subunit of a polymer

Question 14

carbohydrate

Answer 14

has the formula (CH2O)n, ends in -ose, found in ring structures in liquids and chains in solids

Question 15

lipids

Answer 15

mostly C & H, nonpolar

Question 16

protein

Answer 16

chains of amino acids, has the amine group and is polar (positive at nitrogen end, negative at the opposite end where O is)

Question 17

peptide

Answer 17

short protein

Question 18

polypeptide

Answer 18

long protein

Question 19

nucleic acid

Answer 19

nitrogenous base + carbohydrate + phosphate group

Question 20

nitrogenous base

Answer 20

monomer of nucleic acid, Adenine, Thymene, Cytosine, and Guanine

Question 21

polymer of nucleotides

Answer 21

long chain of nucleotides

Question 22

monosaccharide

Answer 22

one carbohydrate molecule

Question 23

alpha- monosaccharide

Answer 23

OH group below the plane of the carbons

Question 24

beta- monosaccharide

Answer 24

OH group above the plane of the carbons

Question 25

starch

Answer 25

disaccharide formed by two or more alpha-saccharide cules

Question 26

cellulose

Answer 26

disaccharide formed by two or more beta-saccharide cules

Question 27

alpha- disaccharide

Answer 27

two monosaccharides joined together by a bond with oxygen below the plane of the carbons

Question 28

beta- disaccharide

Answer 28

two monosaccharides joined together by a bond with oxygen above the plane of the carbons.

Question 29

4 types of biomolecules

Answer 29

carbs, lipids, amino acids, nucleic acids

Question 30

Triglycerides

Answer 30

three fatty acids and a glycerol These are slower to build up and break down than carbs, they're useful for long term energy storage, and they're typically found in fats and oils.

Question 31

Saturated fatty acid

Answer 31

single bonds between carbons, solid at room temperature, found in animal sources, mostly linear

Question 32

Unsaturated fatty acid

Answer 32

one or more double bonds, liquid at room temperature, found in plant sources

Question 33

CIS unsaturated fatty acid

Answer 33

hydrogens are on the same side (looks like a C), appears bent

Question 34

TRANS unsaturated fatty acid

Answer 34

hydrogens on opposite sides (looks like an S), mostly linear, not naturally occurring, bad for you

Question 35

Steroids

Answer 35

backbone of four carbon rings, properties are given by attached functional groups (which can be large)

Question 36

Phospholipids

Answer 36

two fatty acids and a phosphate group attached to glycerol, hydrophobic side, and a hydrophilic side, can assemble into a bubble or a bilayer, has a saturated leg and an unsaturated leg

Question 37

appearance of a phospholipid

Answer 37

phosphate attached to the top carbon of the glycerol on one side through an oxygen, then two fatty acids connected to the bottom two carbons of the glycerol on the opposite side

Question 38

protein

Answer 38

covalently bonded amino acids that form a peptide, which bonds and fold to make a polypeptide. carboxyl group on the C connects to the amine group by losing a water molecule.

Question 39

R groups (proteins)

Answer 39

reactive groups connected to the middle C in the NCC chain, made up of functional groups.

Question 40

4 levels of structure in proteins

Answer 40

primary, secondary, tertiary, and quaternary

Question 41

primary protein structure

Answer 41

first level of organization in proteins. occurs when the DNA is synthesized to form amino acids, which connect to one another covalently.

Question 42

secondary protein structure

Answer 42

the protein begins to have interactions within itself. the carboxyl, hydroxyl, and ketone groups within the amino acids start to interact with one another via H-bonding, causing the structure to curl up in places.

Question 43

tertiary protein structure

Answer 43

R groups of the protein interact further developing the protein's folded structure.

Question 44

quaternary protein structure

Answer 44

R groups of the folded protein interact with the R groups of other folded proteins, creating a ball of proteins.

Question 45

native (normal) proteins

Answer 45

proteins that folded correctly with little to no abnormalities

Question 46

nonnative (toxic) proteins

Answer 46

proteins that folded incorrectly, resulting in the wrong shape and function. these proteins can "infect" normal proteins and cause them to become toxic, leading to the buildup of these proteins and therefore disorders and diseases.

Question 47

diseases caused by toxic proteins

Answer 47

Alzheimer's (caused by amyloids), Parkinson's, Huntington's, diabetes, high cholesterol

Question 48

amyloids (proteins)

Answer 48

toxic protein with an abnormally large amount of beta-pleated sheets.

Question 49

beta-pleated sheets (proteins)

Answer 49

places in the proteins where the chain folds/turns rather than curls

Question 50

functional properties of proteins

Answer 50

storage, transport, enzymes, structure, immune system, motor function, etc

Question 51

which part of the protein is integral for the protein's shape?

Answer 51

R-groups, as they determine how the protein folds up

Question 52

how many common amino acids are used by living things?

Answer 52

20

Question 53

BMI

Answer 53

weight (kg)/height (m^2)

Question 54

hydrogenation

Answer 54

artificial addition of double bonds to oils through a process involving pressure, hydrogen gas, and a nickel catalyst

Question 55

dietary guidelines

Answer 55

avoid trans fats & switch to other fats

Question 56

strengths of using BMI

Answer 56

simple and inexpensive, non-invasive, gives the doctor an idea of what to check for

Question 57

limitations of using BMI

Answer 57

measure of excess weight, not fat; doesn't account for factors like age, sex, ethnicity, height, sexual maturation, and muscle mass; who is BMI based on?