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BIO 102 > Quiz 1 Chap 2&3 > Flashcards

Quiz 1 Chap 2&3 Flashcards

Atoms, Bonds, and Water, and Biological Molecules

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Biology 101 flashcards
1
Q

primordial soup

A

water in oceans many years ago, where life originated

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2
Q

matter

A

made up of elements, containing mass

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3
Q

elements

A

substance that cannot be broken down to other substances by chemical reactions

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4
Q

compounds

A

substance consisting of 2 or more elements in a fixed ratio

- different from the individual elements in its characteristics

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5
Q

how many elements are essential to life? which elements are essential to life?

A

25 elements total, although some are trace elements (minute quantities)

  • 96% of human body. weight is oxygen, carbon, hydrogen, and nitrogen
  • then calcium, phosphorus, potassium, and sulfur
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6
Q

atom

A

smallest unit of an element
composed of subatomic particles (protons, neutrons, electrons)
electrons move around nucleus in orbitals

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7
Q

what does the chemical behavior of an element depend on?

A

the number of UNPAIRED valence elections in the valence shell

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8
Q

molecule

A

atoms that stay close together by chemical bonds (can be 2 of the same atom)

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9
Q

intramolecular forces

A

bonds that hold molecules together (ionic bonds, covalent bonds, polar covalent bonds)

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10
Q

intermolecular forces

A

bonds that hold different molecules together (hydrogen bonds, Van der Waal bonds)

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11
Q

bonding capacity of an element

A

of covalent bonds that each element can form (# of unpaired electrons in the valence shell)

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12
Q

ionic bonds

A
  • give away or steal an electron
  • formed by attraction of two oppositely-charged ions
  • strong in dry environment
  • weak in aqueous environment (water is polar, it splits apart ions)
  • formed by a metal and a non-metal
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13
Q

salts

A

compounds formed by ionic bonds, typically crystals containing huge numbers of cations and anions

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14
Q

covalent bonds

A
  • share valence electrons so that both atoms can fill their valence shells
  • can from between atoms of the same or different elements
  • very strong bonds
  • bonds made and broken from chemical reactions
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15
Q

nonpolar covalent bonds

A

no charges on molecule, atoms share electron(s) equally

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16
Q

polar covalent bonds

A

partial positive and negative charges on each molecule due to the electron not being shared equally (one atom is more electronegative)

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17
Q

hydrogen bonds

A

result of attraction between a partially positive hydrogen (covalently bonded to a more electronegative atom like oxygen) and another electronegative atom

  • what causes water to adhere to itself
  • hydrogen typically bonded to oxygen or nitrogen in living cells
  • weak individually, but many can be strong
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18
Q

role of hydrogen bonds in biological systems

A
  • bonds between nitrogenous bases in DNA, able to be unzipped
  • factor in protein structure
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19
Q

why do substances dissolve in water??

A

water is the universal solvent because of its polarity (oxygen has partial negative, hydrogens have partial positive)

  • ionic bonds broken as ions are attracted to these partial charges
  • large proteins have polar regions on their surfaces which attract water molecules
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20
Q

hydration

A

ionic bonds break and ions attach/come close to polar water molecules

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21
Q

Van der Waals bond

A
  • intermolecular force
  • electrons accumulate randomly in nonpolar molecules (temporary and by chance)
  • individually weak, powerful if occurring simultaneously
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22
Q

which type of bond is strongest?

A

covalent bonds

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23
Q

role of weak bonds (ionic, hydrogen)

A
  • reinforce shape of large molecules

- help molecules adhere to each other

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24
Q

what determines molecular shape?

A

the position of valence orbitals

- orbitals may hybridize in covalent bonds

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25
Q

what is the importance of molecular shape?

A

biological molecules recognize and interact with each other based on shape, so molecules with similar shape can have similar biological effects

  • i.e. morphine and endorphins
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26
Q

significance of water in organisms

A

most cells surrounded by water and are made up of 70-95% water

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27
Q

what 4 properties of water facilitate life processes

A
  1. cohesive behavior
  2. ability to moderate temperature
  3. expansion upon freezing
  4. versatility as a solvent
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28
Q

cohesion

A

hydrogen bonds hold water molecules together

  • causes surface tension
  • helps transport of water against gravity in plants
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29
Q

adhesion

A

attraction between water and other substances

- notably, plant cell walls (again allows for transport up plants)

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30
Q

what is the significance of water’s high specific heat capacity?

A
  • can absorb/release large amounts of heat without changing its own temperature much, which helps maintain HOMEOSTASIS
  • **heat is absorbed when hydrogen bonds break (ice crystals breaking) and released when bonds form
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31
Q

why does water expand when it freezes?

A

hydrogen bonds are more ordered, causing molecules to be farther apart (less dense)

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32
Q

at what temp is water the most dense?

A

4 celsius

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33
Q

why is water a versatile solvent?

A
  • polarity (hydrogen bonds) allow for even large molecules (e.g. proteins) to be dissolved if they have ionic/polar regions
34
Q

hydration shell

A

when each ion in an ionic compound is dissolved in water

35
Q

primary molecules that make up cells

A

carbon-based (organic) compounds

36
Q

why is carbon so important in organic chemistry?

A

it’s tetravalent (4 unpaired valence electrons)

37
Q

hydrocarbons and example of a hydrocarbon

A

organic molecules made up of carbon and hydrogen only (e.g. fats)

38
Q

macromolecule and the 4 classes

A

large organic molecules made up of thousands of covalently connected atoms
- carbohydrates, lipids, proteins, nucleic acids

39
Q

monomer

A

small organic molecule, “building block” of polymers

40
Q

polymer and 3 types of polymers

A

long molecule made up of many similar, smaller units (monomers)
- carbohydrates, proteins, nucleic acids

41
Q

isomers

A

compounds with the same numbers of each atom, but a different configuration

***different structure means different function!!

42
Q

dehydration reaction

A

2 monomers bond together through the loss of a H2O molecule

43
Q

hydrolysis reaction

A

polymer disassembled into monomers, reverse of a dehydration reaction (requires water)

44
Q

main functions of carbohydrates

A

fuel, building material

45
Q

what are monosaccharides and how are they classified?

A

simple sugars–molecular formulas in multiples of CH2O

  • glucose is most common
  • classified by location of carbonyl group (C=O) and # of carbons in skeleton
46
Q

aldoses vs ketoses

A

aldoses have double bonded O on end of carbon chain

ketoses have double bonded O on a middle carbon

47
Q

examples and roles of storage polysaccharides

A

starch

  • plants: granules in chloroplasts and plastids
  • beneficial form of storage compared to lipids because it doesn’t go bad

glycogen
- animals: stored in liver and muscle cells of vertebrates

48
Q

examples and roles of structural polysaccharaides

A

cellulose
- component of tough cell wall in plants, allow them to grow tall

chitin
- found in insect exoskeletons and fungi cell walls

49
Q

difference between cellulose and starch in digestion

A

***both are glucose polymers with different linkages

  • humans can digest alpha linkages of starch, but don’t have enzymes to digest beta linkages of cellulose
  • cellulose passes through digestive tract as insoluble fiber
  • microbes in some herbivores digest cellulose
50
Q

characteristics of lipids and the 3 types

A
  • do not form polymers
  • mostly hydrocarbons that form nonpolar covalent bonds –> hydrophobic
  • generally lighter than water
  • fats, phospholipids, and steroids
51
Q

fats

A

made up of glycerol (3 carbon alcohol with 3 hydroxyl groups) and fatty acids (carboxyl group attached to long carbon skeleton) attached with ester linkage

52
Q

triglyceride

A

3 fatty acids joined to a glycerol by an ester linkage

53
Q

where is fat stored in animals, and what is its role?

A

stored in adipose cells

  • energy storage
  • cushions organs
  • insulates body (warmth)
54
Q

saturated vs unsaturated fatty acids

A

saturated (most animals)

  • max # of hydrogen atoms possible on each carbon
  • no double bonds
  • solid at room temp (with exceptions)

unsaturated (fish, plants)

  • double bonds
  • liquid at room temp
55
Q

what is the danger of excess saturated fats?

A

it can form plaques blocking things like arteries

56
Q

hydrogenation

A

unsaturated fats turned into saturated fats by adding hydrogen to create trans fats

  • hydrogen atoms on opposite sides before/after double bonded carbon
  • even more unhealthy than saturated fats
57
Q

phospholipid structure and purpose

A

2 fatty acids and a phosphate group attached to glycerol

  • fatty acids are hydrophobic, phosphate forms a hydrophilic head
  • major component of all cell membranes
58
Q

what happens when phospholipids are added to water?

A

they self-assemble into a bilayer, with hydrophobic heads pointing interior and phosphate group on the outside

(both interior and exterior of cells are aqueous)

59
Q

structure and function of steroids

A

carbon skeleton consisting of 4 fused rings

  • hormones, metabolism, inflammation, immune functions, salt & water balance, development of sexual characteristics
60
Q

danger of steroids

A

important component of animal cell membranes, but high levels in blood can cause cardiovascular disease

61
Q

protein

A

one or more polypeptides

62
Q

function and importance of proteins

A
  • more than 50% of dry mass of cells
  • structurally diverse (structure determines function)
  • structural support, storage, transport, movement, cellular communications, defense against foreign substances
63
Q

enzymes

A

protein that acts as a catalyst (speeds up chemical reactions)
- perform functions repeatedly

64
Q

polypeptide

A

polymers built from the same set of 20 amino acids

65
Q

amino acid

A

organic molecules with a central carbon, a hydrogen, an amino group, a carboxyl group, and a variable group

66
Q

peptide bonds

A

bonds that link amino acids to form polypeptides

  • formed by a dehydration reaction to connect the carboxyl group of one amino acid with the amino group of another
67
Q

primary protein structure

A

unique sequence of amino acids

68
Q

secondary protein structure

A

(in most proteins) by inherited genetic info, coils and folds in the chain as a result of hydrogen bonds between animo acids

*alpha helices and beta pleated sheets

69
Q

alpha helices vs beta pleated sheets

A

alpha helices are coils, beta pleated sheets have folded structure

70
Q

tertiary protein structure

A

determined by interactions among various side chains (R groups)
- hydrogen bonds, van de waals bonds, ionic bonds, hydrophobic interactions, disulfide bridges (covalent)

71
Q

quaternary protein structure

A

protein consisting of multiple polypeptide chains (i.e. collagen, hemoglobin)

72
Q

what causes sickle cell anemia?

A

a single amino acid substitution (passed on genetically) completely changes the shape

73
Q

other factors determining protein structure

A

alterations in pH, salt concentration, temperature, and environmental factors

74
Q

denaturation

A

protein unravels, losing its native structure

- becomes biologically inactive!

75
Q

how do we determine protein structure (historically and now)?

A
  • x-ray crystallography
  • nuclear magnetic resonance spectroscopy
  • now: bioinformatics (computer programs)
76
Q

what were the two types of bacteria in lab and what were their features?

A

micrococcus luteus - round, gram positive (violet)

E. coli - rod shaped, gram negative (pink)

77
Q

If an antibiotic is effective, the bacteria is _______ to the antibiotic.
If an antibiotic is ineffective, the bacteria is _______ to the antibiotic.

A

susceptible, resistant

78
Q

two types of antibiotics used

  • classes
  • mode of action
  • effective on
A

penicillin

  • B lactam
  • inhibits peptidoglycan layer
  • effective on gram + (micrococcus luteus)

streptomyosin

  • aminoglycocide
  • inhibits protein formation on ribosomal level
  • effective on gram - (E. coli)
79
Q

what techniques did we use in lab?

A

zone of inhibition bioassay and a gram stain

80
Q

why were antibiotics effective/not effective on Gram +/- bacteria?

A

Penicillin targets peptidoglycan layer, so it’s only effective on the gram + cells with a thick peptidoglycan layer.

Streptomyosin targets ribosomal functions but is large in size, so it’s only effective on gram - cells with thinner peptidoglycan layers that it can pass through.

BIO 102 (14 decks)

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