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IBHL Bio - Webb > Biomolecules > Flashcards

Biomolecules Flashcards

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Biology 101 flashcards
1
Q

Adhesion

A

“sticks” to other substances

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2
Q

Cohesion

A

“sticks” to itself

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3
Q

Surface tension is due to

A

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

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4
Q

hydrophobic

A

repels water

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5
Q

hydrophilic

A

attracts water

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6
Q

condensation reaction

A

reaction in which H2O is produced

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7
Q

hydrolysis reaction

A

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.

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8
Q

transpiration

A

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

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9
Q

Some important properties of H2O

A
  • Less dense as a solid
  • Temperature buffer (changes temp slowly and absorbs a lot of nrg)
  • can undergo H2O dissociation
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10
Q

H2O dissociation

A

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

This occurs once in every 10^7 cules

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11
Q

functional groups

A

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

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12
Q

polymer

A

chain of biomolecules

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13
Q

monomers

A

one subunit of a polymer

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14
Q

carbohydrate

A

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

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15
Q

lipids

A

mostly C & H, nonpolar

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16
Q

protein

A

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

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17
Q

peptide

A

short protein

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18
Q

polypeptide

A

long protein

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19
Q

nucleic acid

A

nitrogenous base + carbohydrate + phosphate group

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20
Q

nitrogenous base

A

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

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21
Q

polymer of nucleotides

A

long chain of nucleotides

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22
Q

monosaccharide

A

one carbohydrate molecule

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23
Q

alpha- monosaccharide

A

OH group below the plane of the carbons

24
Q

beta- monosaccharide

A

OH group above the plane of the carbons

25
Q

starch

A

disaccharide formed by two or more alpha-saccharide cules

26
Q

cellulose

A

disaccharide formed by two or more beta-saccharide cules

27
Q

alpha- disaccharide

A

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

28
Q

beta- disaccharide

A

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

29
Q

4 types of biomolecules

A

carbs, lipids, amino acids, nucleic acids

30
Q

Triglycerides

A

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.

31
Q

Saturated fatty acid

A

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

32
Q

Unsaturated fatty acid

A

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

33
Q

CIS unsaturated fatty acid

A

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

34
Q

TRANS unsaturated fatty acid

A

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

35
Q

Steroids

A

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

36
Q

Phospholipids

A

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

37
Q

appearance of a phospholipid

A

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

38
Q

protein

A

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.

39
Q

R groups (proteins)

A

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

40
Q

4 levels of structure in proteins

A

primary, secondary, tertiary, and quaternary

41
Q

primary protein structure

A

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

42
Q

secondary protein structure

A

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.

43
Q

tertiary protein structure

A

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

44
Q

quaternary protein structure

A

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

45
Q

native (normal) proteins

A

proteins that folded correctly with little to no abnormalities

46
Q

nonnative (toxic) proteins

A

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.

47
Q

diseases caused by toxic proteins

A

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

48
Q

amyloids (proteins)

A

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

49
Q

beta-pleated sheets (proteins)

A

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

50
Q

functional properties of proteins

A

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

51
Q

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

A

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

52
Q

how many common amino acids are used by living things?

A

20

53
Q

BMI

A

weight (kg)/height (m^2)

54
Q

hydrogenation

A

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

55
Q

dietary guidelines

A

avoid trans fats & switch to other fats

56
Q

strengths of using BMI

A

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

57
Q

limitations of using BMI

A

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?

IBHL Bio - Webb (6 decks)

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