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BIL 150 > Exam #2 > Flashcards

Exam #2 Flashcards

1
Q

ionic bond

A

transfer of electrons between atoms; electrostatic attraction of ionized molecules

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2
Q

covalent bond

A

the sharing of electrons between atoms

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3
Q

glycosidic bond

A

oxygen bridging glucoses together; has alpha and beta orientations - alpha (hydroxyl group [OH] down) vs. beta (hydroxyl group [OH] up on one side)

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3
Q

hydrogen bond

A

weak electrostatic attraction between molecules; not very strong, but can form many at a time

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4
Q

ester bond

A

links fatty acids and glycerol in fats; creates fat molecule by forming a triglyceride

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5
Q

phosphodiester bond

A

phosphate link between sugars of nucleotides; forms through condensation reaction that removes water molecule and forms a bond, creating the sugar-phosphate backbone of DNA

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6
Q

amino functional group

A

-NH2; amino acid - weak base

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7
Q

name of amino functional group compound

A

amine (ex: glycine, which is also a carboxylic acid)

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8
Q

functional properties of amino group

A

acts as base; can pick up an H+ ion from surrounding solution

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9
Q

how many functional groups are there? name them

A

7: amino, carbonyl, carboxyl, methyl, hydroxyl, phosphate, sulfhydryl

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10
Q

carbonyl functional group

A

-C=O; ketones and aldehydes; structural isomers

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11
Q

what indicates a ketone?

A

if the carbonyl group is located within a carbon skeleton

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12
Q

what indicates an aldehyde?

A

if the carbonyl group is located at the end of the carbon skeleton

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13
Q

Ketose sugars

A

fructose

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14
Q

Aldose sugars

A

glucose

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15
Q

carboxyl functional group

A
  • COOH; double bond between C and O (C=O), acidic properties due to high polarity, anion w/ minus 1 charge
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16
Q

hydroxyl functional group

A

-OH (or HO); forms alcohols, polar due to electrons being drawn more towards O atom (it has higher electronegativity), can form H bonds w/ water molecules

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17
Q

methyl functional group

A

-CH3 or H3C; all single bonds w/ C at the center; adding methyl to DNA or DNA-bound molecule can impact gene expression

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18
Q

phosphate functional group

A

-PO4; double bond formed between P and the O atom directly above it, contributes negative charge to molecule, potential to react w/ water and release energy

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19
Q

sulfhydryl functional group

A

-SH or HS; 2 can react to form covalent bond (“cross-linking” stabilizes protein structure)

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20
Q

what is a protein?

A

a species-specific polymer of amino acids w/ biological activity

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21
Q

why are proteins important?

A

all life depends on proteins; they provide cellular structure and mediate nearly all cellular functions

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22
Q

how does a protein form?

A

amino acids join to form polypeptide chains, moving from monomer to polymer status

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23
Q

how many sets of amino acids are there?

A

20

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24
Q

what is the structure of an amino acid?

A

an amino group (NH2), a carboxyl group (COOH), a hydrogen atom (H), and a variable “R” group that dictates uniqueness; all attached to a central carbon atom

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25
Q

what are the different levels of protein structure?

A

primary, secondary, tertiary, and quaternary

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26
Q

primary structure

A

the linear string of amino acids, the initial sequence

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27
Q

secondary structure

A

portions of linear chain may fold into an alpha helix OR fold back and forth into beta-pleated sheets; held together by hydrogen bonds

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28
Q

tertiary structure

A

overall shape of the protein, takes on 3D structure, results from interactions between R groups

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29
Q

quaternary structure

A

two or more polypeptide chains aggregated into one functional protein

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30
Q

what is denaturation?

A

the process in which a protein loses its function due to physical or chemical changes in the environment –> cause the protein to unravel

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31
Q

what are the different types of proteins?

A

enzymes, transport, storage, defensive, contractile, hormone-signal, receptor, structural

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32
Q

enzyme

A

protein that catalyzes chemical reactions (speeds them up by lowering amount of energy used)
ex: digestive enzymes

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33
Q

transport

A

transport substances around a cell and/or across cell membrane
ex: hemoglobin

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34
Q

storage

A

store amino acids (ex: casein, ovalbumin in egg white)

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35
Q

defensive

A

protect against disease and viruses, aid immune system (ex: antibodies)

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36
Q

contractile

A

promote movement, help form muscles, tendons, cytoskeletons (ex: actin and myosin)

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37
Q

structural

A

provide structure and support (ex: keratin, collagen)

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38
Q

hormone-signal

A

coordinate physiological activities (ex: insulin regulates blood sugar levels)

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39
Q

receptor

A

respond to stimuli (ex: nerve cell receptors)

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40
Q

building blocks of life

A

monomers; amino acids, nucleotides, fatty acids, carbohydrates/sugars

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41
Q

what polymer do amino acids form?

A

proteins, through polypeptide chains

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42
Q

what polymer do nucleotides form?

A

DNA and RNA (nucleic acids)

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43
Q

what polymer do fatty acids form?

A

lipids and fats

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44
Q

what polymer do sugars form?

A

carbohydrates, including disaccharides and polysaccharides

45
Q

what are the 3 different kinds of isomers?

A

structural, geometric, optical

46
Q

structural isomer

A

same empirical formula, different molecular structure due to atoms being arranged differently

47
Q

geometric isomer

A

cis-trans; cis is same (x’s are on same side) trans is different (x’s are on opposite sides)

48
Q

optical isomer

A

bend the plane of light in different directions; enantiomers create mirror images that cannot be superimposed onto each other

49
Q

cofactor

A

small molecules that bind with enzymes and are necessary for enzyme catalytic function; larger molecules are coenzymes

50
Q

conformation

A

any of the spatial arrangements of a molecule that can be obtained by rotation of the atoms about a single bond

51
Q

enzyme inhibitors

A

selectively disrupt the action of enzymes, either by reversibly binding with the enzyme via weak electrostatic bonds or by irreversibly attaching often via covalent bonds

52
Q

competitive inhibitor

A

competes w/ enzyme by binding at the active site

53
Q

noncompetitive inhibitor

A

competes w/ enzyme by binding to a non-active, or allosteric, site; changes the conformational shape of the enzyme, impeding function

54
Q

chaperone proteins (heat shock proteins)

A

help the intracellular folding of proteins; protect other proteins by changing their shapes and conformations

55
Q

globular protein

A

any protein with a round, ball-like 3D shape

56
Q

allosteric regulation

A

regulation of enzyme activity by the binding of a regulator molecule to an allosteric site, a receptor site separate from the active site

57
Q

fibrous proteins

A

a protein with an elongated shape; form long, filamentous structures (ex: collagen)

58
Q

Purines

A

one category of nitrogen-containing hetero-cyclic ring (2 rings) compounds found in DNA and RNA

59
Q

Pyrimidines

A

other category of nitrogen-containing cyclic ring (1 ring) compounds found in DNA and RNA (ex: adenine, thymine, guanine, cytosine, uracil (replaces T in RNA))

60
Q

double helix

A

the typical conformation of a DNA molecule in which two strands are would around each other with hydrogen bonding base-pairing between the two strands

61
Q

how is an ester formed?

A

when an alcohol combines w/ an acid in a reaction to form an organic compound

62
Q

what is Km?

A

the substrate concentration at which the reaction rate is at half Vmax (half of Vmax)

63
Q

isoelectric point

A

the point on the pH scale in which a molecule exists at a neutral charge (zero charge)

64
Q

what bonds are associated w/ water and how do they form?

A

hydrogen bonds; form when the (+) end of water molecule attracts the (-) side of another

65
Q

cohesion

A

the attachment of water molecules to each other by hydrogen bonding

66
Q

surface tension

A

a measure of how difficult it is to stretch or break the surface of a liquid; water has a very high surface tension

67
Q

adhesion

A

the tendency of water to stick to other substances

68
Q

heat capacity

A

the amount of heat required, in calories, to raise the temperature of one gram of a substance by 1.0℃; the ability of a substance to take in or give up a specific amount of heat and experience large or small changes in temperature

69
Q

heat capacity of pure water

A

high heat capacity; 1.00 cal/g/degrees C

70
Q

calorie

A

one calorie is the amount of heat needed to raise 1 gram of pure water by 1℃

71
Q

thermal inertia

A

how long it takes something to approach the temperature of its surroundings; water has high thermal inertia, so takes longer to heat or cool relative to land

72
Q

viscosity

A

a measure of a fluid’s resistance to flow that describes the internal friction of a moving liquid; how resistant a liquid is to flowing under stress

73
Q

melting point of ice

A

0 degrees C

74
Q

How much heat must be added to raise one gram of water from 0℃ to 100℃ ?

A

To raise one gram of water from 0℃ freezing point to 100℃ boiling point, need to add 100 calories of heat

75
Q

Latent Heat of Vaporization

A

heat added to or removed from a liquid during evaporation or condensation that produces a change in state but NOT a change in temperature

76
Q

what is the latent heat of vaporization of water?

A

540 cal/gram

77
Q

what is the pH scale?

A

a numerical method for expressing the range of H+ concentrations; indicates how many H+ ions are present

78
Q

3 most common shapes of bacteria

A

cocci (spherical), bacillus (rod-shaped), and spirochetes (spiral)

79
Q

gram-staining

A

method for differential staining of bacteria; gram-positive stains purple-black, while gram-negative stains pink

80
Q

gram-positive cell walls contain what?

A

peptidoglycans (protein + carbohydrates)

81
Q

gram-negative walls

A

thinner, more membrane-like = lipopolysaccharides

82
Q

peptidoglycans

A

polysaccharides consisting of sugars and amino acids

83
Q

some pathogenic bacteria

A

cholera, b. coli, tuberculosis, typhoid, tetanus

84
Q

chromosomes

A

“colored bodies” containing genetic information

85
Q

2 major kinds of eukaryotic cells

A

metazoan cell and metaphyta cell

86
Q

Metazoan cell

A

animal; heterotrophic metabolic feeder; NO chloroplast, cell wall, central vacuole, tonoplast, or plasmodesmata

87
Q

Metaphyta cell

A

plant; autotrophic producer; NO lysosomes, centrioles, or flagella

88
Q

importance of light microscope

A

allows for magnification of images up to 1000x

89
Q

optical microscopy

A

involves diffraction, refraction, or dispersion of light interacting w/ live or prepared samples to magnify images of small objects

90
Q

dispersion

A

separation of light into wavelengths via a prism

91
Q

diffraction

A

change in direction of light waves through an opening or around a barrier in a light path

92
Q

how are samples acquired and preserved?

A

killed and fixed; fixation preserves tissues and prevents degradation by forming covalent bonds within and between proteins

92
Q

refraction

A

changes in direction of light waves as they pass from one medium to another

93
Q

spur cell

A

red blood cell w/ spike-like projections that vary in length, width, and distribution

94
Q

Microtome

A

tool used for embedding and sectioning samples (1 to 10 micrometer thick tissue sections)

95
Q

selective staining

A

stains (dyes) attach to specific molecules, colorizing them

96
Q

carbohydrates

A

structure and energy molecules

97
Q

lipids

A

fats; structure and energy molecules; diverse group of hydrophobic molecules

98
Q

proteins

A

wide array of functions and different structures

99
Q

nucleic acids

A

store, transmit, and help express hereditary information

100
Q

phospholipids

A

membrane structure (phospholipid bilayer, one side hydrophilic, the other hydrophobic due to hydrophobic tails)

101
Q

steroids

A

sterols; membrane structure, specially w/ hormones

102
Q

configuration

A

permanent geometry of a molecule resulting from spatial arrangements of covalent bonds in space; more strict/rigid

103
Q

conformation

A

the surface outline or contours/3D structure of molecule, results without breaking any bonds due to free rotation about single bond and weak electrostatic forces; more free and passive

104
Q

4 basic parts of cell

A

membrane, DNA region, protoplasm/cytoplasm, organelles

105
Q

Cell membrane

A

selectively permeable; chooses what is allowed inside and outside of the cell while also differentiating in from out

106
Q

DNA region

A

eukaryotes store DNA in the nucleus (control center), prokaryotes store DNA in nucleoid

107
Q

Organelles

A

“mini organs” that are designed to perform specific functions to help the cell responsible for cellular respiration and ATP production)

108
Q

Protoplasm/Cytoplasm

A

aqueous solution providing structure and form to cells; also called cytosol

BIL 150 (3 decks)

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