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bio 112 > unit one > Flashcards

unit one Flashcards

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Biology 101 flashcards
1
Q

what are the basic qualities about cells?

A
  • cells can vary in size and structure
  • can be both an organism and part of an organism
  • multiple cells make up specialized tissues and organs
  • unicellular organisms have to carry out all the functions with their one cell
  • most cells are self-replicating, with the exception of neurons, gametes, and red blood cells
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2
Q

what does self-replicating mean?

A

cells reproducing themselves to create an identical copy

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3
Q

what are the criteria for a cell to be self-replicating?

A
  • have DNA and a way to replicate it
  • a way to read the DNA
  • energy source
  • raw materials
  • plasma membrane
  • way to replicate other organelles and cell materials
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4
Q

what is the cell theory?

A

1) all living organisms are made up of cells
2) cells are the basic unit of life
3) cells arise from pre-existing cells
4) hereditary info is passed from cell-to-cell
5) all cells have the basic chemical composition
6) energy flow occurs within cells

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5
Q

what is a prokaryotic cell?

A

they have no membrane-bound organelles

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6
Q

what is a eukaryotic cell?

A

they have membrane-bound organelles

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7
Q

what is the main differences between prokaryotic and eukaryotic cells?

A
  • eukaryotes have membrane bound organelles
  • prokaryotes have no mitochondria, or nucleus
  • prokaryotes are smaller than eukaryotes
  • prokaryotes are more primitive than eukaryotes
  • prokaryotes have circular DNA present in the nucleoid, eukaryotes have linear DNA present in the nucleus
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8
Q

what are the types of bonds?

A
  • covalent bonds
  • non-covalent bonds
  • polar covalent bonds
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9
Q

what is a covalent bond?

A

intramolecular bond
stronger and more permanent

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10
Q

what is a non-covalent bond?

A

intermolecular bond
weaker and less permanent
lots of non-covalent bonds hold molecules together

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11
Q

what is a polar covalent bond?

A

unequal sharing of electrons due to a difference in electronegativity

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12
Q

what is the electronegativity scale order?

A

O > N&raquo_space; S > C = H = P

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13
Q

if a molecule is polar, is it hydrophilic or hydrophobic?

A

hydrophilic

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14
Q

if a molecule is non-polar, is it hydrophilic or hydrophobic?

A

hydrophobic

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15
Q

what is the main type of non-polar bond?

A

C-H bond

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16
Q

what is an induced dipole?

A

non-polar

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17
Q

what is a permanent dipole?

A

polar

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18
Q

what is the basis of organic molecules?

A

must have at least 1 C-H bond

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19
Q

what are the 4 major macromolecules?

A
  • carbohydrate
  • protein
  • nucleic acid
  • lipid
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20
Q

what are carbohydrates used for?

A

energy source

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21
Q

what are proteins used for?

A

enzymes, structure, support

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22
Q

what are nucleic acids used for?

A

DNA and RNA

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23
Q

what are lipids used for?

A

cell membrane

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24
Q

what three macromolecules exhibit polarity?

A

carbohydrates, proteins, and nucleic acids

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25
Q

what does polarity mean in terms of macromolecules?

A

the polymer has two chemically distinct ends

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26
Q

what is the general structure of a protein?

A
  • N terminus and C terminus
  • alpha carbon
  • R group
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27
Q

what is the directionality of a protein?

A

N to C

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28
Q

what is the monomer of proteins?

A

amino acid

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29
Q

what is the bond in a protein called?

A

peptide bond

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30
Q

what is the general structure of a nucleic acid?

A
  • phosphate group
  • 5 carbon ring
31
Q

what is the directionality of a nucleic acid?

A

5’ to 3’

32
Q

what is the monomer of a nucleic acid?

A

nucleotide

33
Q

what is the bond in a nucleic acid called?

A

phosphodiester bond

34
Q

what is the monomer of a carbohydrate?

A

monosaccharide

35
Q

what is the bond in a carbohydrate?

A

glycosidic bond

36
Q

why are lipids different?

A

they are defined by their properties more than their structure
(typically very hydrophobic)

37
Q

what is the monomer of lipids?

A

fatty acids

38
Q

what is the bond in a lipid?

A

ester linkage

39
Q

what is the general structure of a lipid?

A

a non-identical molecule (head group) attached to the monomer chains (tail)

40
Q

what is the general structure of a phospholipid?

A
  • two non-polar hydrophobic fatty acid tails
  • polar, hydrophilic, phosphate head
  • glycerol backbone
41
Q

what are the three types of phospholipid arrangements? describe each.

A
  • bilayer: smaller head, double tails
  • liposome: mixed lipids, some double tails
  • micelle: bulkier head, single tail
42
Q

what is molecular self-assembly?

A

when molecules form a particular 3D conformation or structure

43
Q

why does molecular self-assembly occur?

A

1) interaction with surrounding water molecules
2) intermolecular interactions
3) intramolecular interactions
- it is more thermodynamically favourable to be in that structure

44
Q

describe phospholipid self-assembly in water.

A
  • spontaneous (self-healing)
  • energetically favourable
  • gibbs free energy is less than 0
  • system shifts from less stable to more stable
45
Q

what is the hydrophobic effect?

A

allowing hydrophobic / non-polar molecules to clump together thereby increasing the entropy of the water

46
Q

what is the largest contributor to bilayer stability?

A

although both entropy and enthalpy contribute to bilayer stability, entropy is the largest contributor

47
Q

what does it mean by the selective barrier of the cell membrane?

A

the lipid bilayer of semi-permeable, it has a selective barrier - only allows small, non-polar molecules through.

48
Q

why does the cell have a selective barrier?

A

to help maintain homeostasis

49
Q

what are the 2 types of transport?

A

passive and active

50
Q

what is passive transport?

A
  • diffusion
  • goes along the conc gradient
  • no input of energy
  • move in both directions
51
Q

what are the two types of diffusion?

A

simple diffusion and facilitated diffusion

52
Q

what is simple diffusion?

A

diffusions through the bilayer

53
Q

what is osmosis?

A

the diffusion of water to make the conc of solute equal

54
Q

what is facilitated diffusion?

A

uses a transport protein to diffusion across the bilayer. can be with a channel protein, or a carrier protein

55
Q

what is facilitated diffusion using a channel protein?

A
  • open or gated
  • diffuse through the channel
  • for ions and small polar/ non-polar molecules
  • hydrophilic pathway
  • faster than carrier mediated
  • molecules interact with protein for it to be transported
56
Q

what is facilitated diffusion using a carrier protein?

A
  • gated
  • more specific than channel proteins
  • protein undergoes conformational changes to open and close the protein
57
Q

what is active transport?

A

requires energy to go against the concentration gradient. there is primary and secondary

58
Q

what is primary active transport?

A
  • energy is required to directly move a molecule from one side of the membrane
59
Q

what is secondary active transport?

A
  • energy is required to build up the concentration of different molecules
  • creates an electrochemical gradient
  • diffusion of the molecule along the gradient is used to power the movement of the molecule
  • ATP used to pump H+ out
60
Q

how is the bilayer described as?

A

fluid mosaic model

61
Q

what are integral membrane proteins?

A

permanently associated with the cell membrane and cannot be separated from the membrane experimentally without destroying the membrane itself
- most are transmembrane proteins (span the entire bilayer)
- embedded in the membrane

62
Q

what are peripheral membrane proteins?

A

temporarily associated with the lipid bilayer or with integral membrane proteins through non-covalent interactions
- easily separated
- associated with either the internal or external side
- not embedded in the membrane

63
Q

what is a peptide?

A

short chain of <50 amino acids

64
Q

what is a polypeptide?

A

long chain of amino acids

65
Q

what is a protein?

A

folded chain of amino acids

66
Q

what is amino acyl residue?

A

amino acids with either H or OH removed in the process of peptide bond formation

67
Q

what is the backbone of an amino acid?

A

everything but the R group
- atoms that make up the covalent linkages from one amino acid to the next

68
Q

what does the sequence of amino acids decide?

A

sequence - structure - function

69
Q

what are the four levels of structures for a protein?

A

primary, secondary, tertiary, quatrenary

70
Q

what is primary structure of a protein?

A
  • sequence of amino acids
  • ultimately dictates function
71
Q

what is the secondary structure of a protein?

A
  • results from interactions of nearby amino acids
  • interaction between backbone
  • stabilized by hydrogen bonds between backbone
  • 2 types: alpha helices and beta sheets
72
Q

what is the tertiary structure of a protein?

A
  • 3D structure (fold) of entire polypeptide stabilized by side-chain interactions (non-covalent and disulfide) as well as interactions between sidechains and backbone
  • when it truly becomes a protein
73
Q

what is quatrenary structure?

A
  • multiple folded polypeptide chains
  • stabilized by non-covalent interactions
  • not all proteins have this structure
74
Q

what is protein denaturation?

A

a change in temp, pH, etc. that will cause a protein to unfold

bio 112 (2 decks)

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