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BSC 322 > Exam 1 > Flashcards

Exam 1 Flashcards

1
Q

What is cell theory?

A
  • all living organisms are made up of cells
  • cells are the most basic organizational units
  • all cells come from preexisting cells
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2
Q

what are some advantages of phase contrast over bright field?

A
  • increased contrast
  • higher magnifications
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3
Q

how do you improve the resolution of a light microscope?

A

adjust the course and fine focus

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4
Q

characteristics of carbon

A
  • valence of 4
  • most likely to bond with oxygen, hydrogen, nitrogen, and sulfur
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5
Q

how are covalent bonds formed?

A

by the sharing of a pair of electrons between two atoms

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6
Q

what is electronegativity

A

an atom’s tendency to attract electron to itself in a chemical bond

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7
Q

what makes water a versatile solvent?

A

its charges are really efficient at breaking other molecules up

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8
Q

non-polar bonds

A

share electrons equally

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9
Q

polar bonds

A

share electrons unequally

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10
Q

phosphodiester bonds

A

covalent bonds that link the 5’ phosphate group of one nucleotide to the 3’ hydroxyl group of another

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11
Q

glycosidic bond

A

covalent bonds that connect a carbohydrate molecule to another molecule

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12
Q

Dehydration reaction

A

a chemical reaction that involves the removal of a water molecule, allowing two molecules to bond together

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13
Q

Hydrolysis reaction

A

a chemical reaction that involves the addition of water to break a bond in a polymer, splitting it into smaller units

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14
Q

peptide bonds

A

covalent bonds formed between the carboxyl group of one amino acid and the amino group of another

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15
Q

Virus

A

a microscopic infectious agent that can replicate only inside the living cells of an organism

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16
Q

Viroid

A

a small, circular piece of RNA that is infectious and can cause disease in plants. Lacks a protein coat

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17
Q

Allosteric inhibition

A

a mechanism where a molecule binds to a site other than the active site on an enzyme. causes a change in shape and reduces the enzyme’s activity

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18
Q

feedback inhibition

A

a process in which the end product of a metabolic pathway inhibits an earlier step in the pathway

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19
Q

Michaelis Constant (Km)

A

a measure of the substrate concentration at which an enzyme-catalyzed reaction proceeds at half its maximum velocity

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20
Q

Vmax

A

the maximum rate of an enzyme-catalyzed reaction when the enzyme is saturated with substrate

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21
Q

Endosymbiont theory

A

the origin of mitochondria and chloroplasts evolved from free-living prokaryotic cells that were engulfed by ancestral eukaryotic cells

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22
Q

how does an ionic bond form?

A

when one atoms donates an electron to another atom

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23
Q

features of hydrocarbons

A

organic compounds
composed of only C and H
can be linear or branched

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24
Q

describe amino acid structure

A

central carbon atom bonded to an amino group, a carboxyl group, a H atom, and an R-group (side chain)

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25
Q

Types of R-groups

A
  • can be nonpolar (hydrophobic),
  • polar (hydrophilic),
  • acidic (negatively charged, or
  • basic (positively charged)
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26
Q

directionality in cell biology

A

refers to the orientation of biological molecules

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27
Q

Primary protein structure

A

linear sequence

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28
Q

secondary protein structure

A

local folding patterns

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29
Q

tertiary structure

A

overall 3D shape of a protein

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30
Q

what forms links in polysaccharides

A

glycosidic bonds

31
Q

what kind of bonding for sugars

A

glycosidic

32
Q

functions of sugars

A

serve as immediate energy sources

33
Q

Hydroxyl group

A

polar, forms H bonds, increases solubility

34
Q

carbonyl group

A

can be an aldehyde or ketone

35
Q

carboxyl group

A

acts as an acid (donates H+) polar, and hydrophilic

36
Q

amino group

A

acts as a base (accepts H+), polar, and hydrophilic

37
Q

sulfhydryl group

A

can form disulfide bonds, slightly polar

38
Q

membrane proteins

A

proteins embedded in or associated with the lipid bilayer

39
Q

principle of synthesis by polymerization

A

Monomers make covalent bonds, form polymers via dehydration reactions

40
Q

self-assembly

A

the process by which molecules automatically organize into structures arrangements without external guidance

41
Q

covalent bonds

A

strongest, include disulfide bridges

42
Q

ionic bonds

A

attractions between positively and negatively charged side chains

43
Q

hydrophobic interactions

A

nonpolar R-groups aggregate to avoid water, driving protein folding

44
Q

van der waals forces

A

weak attractions between closely positioned nonpolar molecules, stabilizing protein structure

45
Q

DNA

A

double helix, contains thymine and has a stable structure

46
Q

RNA

A

single stranded, ribonucleic acid, contains uracil, less stable

47
Q

Nucleotide structure

A

composed of a phospate group, a sugar, and a nitrogenous base

48
Q

saturated fatty acids

A

no double bonds, solid at room temp

49
Q

unsaturated fatty acids

A

one or more double bonds, liquid at room temp

50
Q

trans fats

A

unsaturated with trans configuration

51
Q

phospholipids

A

composed of 2 fatty acids and phosphate group

52
Q

steroids

A

lipids characterized by a carbon skeleton of four fused rings

53
Q

golgi apparatus

A

stack of membrane-bound vesicles that modify, sort, and package proteins and lipids for secretion or delivery to organelles

54
Q

lysosomes

A

membrane-bond organelles containing digestive enzymes. break down waste and cellular debris

55
Q

first law of thermodynamics

A

energy cannot be created or destroyed

56
Q

second law of thermodynamics

A

in any energy transfer, entropy increases

57
Q

endergonic

A

require energy input. non-spontaneous

58
Q

exergonic

A

release energy, spontaneous

59
Q

amylase

A

catalyzes the breakdown of starch into sugars

60
Q

DNA polymerase

A

catalyzes the synthesis of DNA during replication

61
Q

catalase

A

breaks down hydrogen peroxide into water and oxygen

62
Q

activation energy

A

min energy required for a chemical reaction to occur

63
Q

transition state

A

an unstable state that occurs during the transformation of reactants to products, characterized by a peak in energy

64
Q

hydrolases

A

catalyze hydrolysis reactions

65
Q

oxidoreductases

A

catalyze redox reactions

66
Q

transferases

A

transfer functional groups between molecules

67
Q

lyases

A

catalyze the addition or removal of groups to form double bonds

68
Q

isomerases

A

catalyze isomerization reactions

69
Q

ligases

A

catalyze the joining of two molecules with the use of ATP

70
Q

cofactors

A

assist enzyme activity by stabilizing structures or participating in the reaction

71
Q

coenzymes

A

act as carries for chemical groups or electrons during enzymes-catalyzes reactions

72
Q

Michaelis plot

A

[substrate] increased = rxn rate increased

73
Q

lineweaver-burke plot

A

double reciprocal plot

BSC 322 (2 decks)

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