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Anatomy & Physiology I > Chapter 2: Chemistry of Life > Flashcards

Chapter 2: Chemistry of Life Flashcards

1
Q

simplest form of matter to have unique chemical properties

A

element

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2
Q

represents the number of protons in its nucleus

A

atomic number

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3
Q

total mass of protons and neutrons

A

atomic mass

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4
Q

has a + charge, 1 amu

A

proton

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5
Q

no charge, mass 1 amu

A

neutron

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6
Q
  • charge, negligible mass
A

electron

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7
Q

atoms with different number of neutrons

A

isotopes

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8
Q

unstable isotopes that give off radiation

A

radioisotopes

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8
Q

charged particles with unequal number of protons and electrons

A

ions

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8
Q

transfer of electrons

A

ionization

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9
Q

atom that gains electrons

A

anion

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10
Q

atom that loses electrons

A

cation

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11
Q

salts that ionize in water; form solutions capable of conducting electric current

A

electrolytes

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12
Q

importance of electrolytes

A

1.Chemical reactivity
2.Osmotic Effects
3.Electrical effects on nerve & muscle tissue

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13
Q

chemical particles with odd number of electrons

A

free radicals

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14
Q

free radicals are produced by…

A

normal metabolic reactions, radiation, chemicals

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15
Q

neutralize free radicals

A

antioxidants

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16
Q

chemical particles composed of two or more atoms united by a chemical bond (ex: H2, O2, H20, C6H12O6)

A

molecules

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17
Q

molecules composed of two or more different elements (ex: H2O, C6H12O6, urea)

A

compounds

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18
Q

bond formed by attraction of cations and anions

A

ionic bond

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19
Q

bond formed by one shared pair of electrons

A

single covalent bond

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20
Q

bond formed by two shared pairs of electrons

A

double covalent bond

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21
Q

bond where electrons are shared equally

A

non-polar covalent bond

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22
Q

bond where electrons are shared unequally

A

polar covalent bond

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23
Q

bond formed with Hydrogen; mostly within water molecules

A

hydrogen bonds

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24
Q

weak, brief attractions between neutral atoms

A

Van der Waals forces

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25
Q

molecules with identical molecular formulas but different arrangement of their atoms

A

isomers

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26
Q

substances physically blended, but not chemically combined

A

mixture

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27
Q

the ability for water to stick to other molecules

A

adhesion

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28
Q

the ability for water to stick to itself; causes surface tension

A

cohesion

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29
Q

ability to dissolve other chemicals

A

solvency

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30
Q

the universal solvent

A

water

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31
Q

particles in water that cannot be seen

A

solution

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32
Q

particles stay suspended, but do not separate out on standing; cloudy/translucent

A

colloid

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33
Q

particles are too large that it separates on standing; cloudy/opaque

A

suspension

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34
Q

water’s ability to participate in chemical reactions

A

chemical reactivity

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35
Q

helps water stabilize internal temperature of the body

A

thermal stability

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36
Q

of moles of solute per liter in a solution

A

molarity

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37
Q

proton donor (releases H+ ions)

A

acid

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38
Q

proton acceptor (accepts H+ ions)

A

base

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39
Q

pH 7.0

A

neutral

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40
Q

pH > 7.0

A

basic

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41
Q

pH< 7.0

A

acidic

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42
Q

resists change in pH

A

buffers

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43
Q

What is the pH of blood?

A

7.35-7.45

44
Q

process in which covalent or ionic bond formed or broken

A

chemical reactions

45
Q

large molecule breaks down into two or more smaller ones

A

decomposition

46
Q

two or more small molecules combine to form a larger

A

synthesis reaction

47
Q

two molecules exchange atoms or groups of atoms

A

exchange reaction

48
Q

reaction that can go either way

A

reversible reaction

49
Q

reactions that break covalent bonds, exergonic, decomposition

A

catabolism

50
Q

energy releasing reactions

A

exergonic

51
Q

reactions that store energy, endergonic, synthesis reaction; REQUIRES energy input

A

anabolism

52
Q

energy using reactions

A

endergonic

53
Q

a molecule that gives up electrons; releases energy

A

oxidation

54
Q

electron donor

A

reducing agent

55
Q

a molecule that gains electrons; gains energy

A

reduction

56
Q

electron acceptor

A

oxidizing agent

57
Q

study of compounds containing carbon

A

organic chemistry

58
Q

four categories of carbon compounds

A

carbohydrates, lipids, proteins, nucleic acids

59
Q

small molecules that can react with other molecules to form large/complex molecules

A

monomers

60
Q

molecules made of repetitive series of identical similar subunits (monomers)

A

polymers

61
Q

determines properties of organic molecules

A

functional groups

62
Q

joining monomers to form a polymer; formed by dehydration synthesis

A

polymerization

63
Q

splitting polymer (LYSIS) by adding water molecules

A

hydrolysis

64
Q

hydrophilic organic molecule

A

carbohydrates

65
Q

glucose, galactose, fructose

A

monosaccharide

66
Q

sucrose, lactose, maltose (made of two monosaccharides)

A

disaccharides

67
Q

short chains of monosaccharides (3 or more)

A

oligosaccharides

68
Q

long chains of monosaccharides (50 or more)

A

polysaccharides

69
Q

energy storage polysaccharide in human tissue

A

glycogen

70
Q

energy storage polysaccharide in plants

A

starch

71
Q

structural molecule of plants cell walls

A

cellulose

72
Q

hydrophobic organic molecules

A

lipids

73
Q

no H+ can be added (solid at room temperature)

A

saturated fatty acids

74
Q

has double bond (liquid at room temperature)

A

unsaturated fatty acids

75
Q

resists enzymatic breakdown, circulates longer, deposits in arteries

A

trans-fatty acids

76
Q

found naturally in food; beneficial

A

cis-fatty acids

77
Q

three fatty acids covalently bonded to glycerol; bond formed by dehydration synthesis

A

triglycerides

78
Q

solid triglyceride at room temperature

A

fats

79
Q

liquid triglyceride at room temperature

A

oils

80
Q

one fatty acid replaced by a phosphate group

A

phospholipid

81
Q

both water fearing and loving

A

amphiphilic

82
Q

derived from arachidonic acid; hormone like chemical signals between cells

A

eicosanoids

83
Q

good proteins, lower ratio of lipids to proteins

A

high density lipoproteins

84
Q

bad proteins, high ratio of lipid to proteins

A

low density lipoproteins

85
Q

polymer of amino acids

A

proteins

86
Q

amino acids have a central carbon with one of these attachments

A

amino, carboxyl, radical

87
Q

loss of conformation and function of a protein

A

denaturation

88
Q

linear sequence of amino acids

A

primary structure

89
Q

pattern caused by interaction in nearby amino acids, helix or pleated sheet

A

secondary structure

90
Q

connections between amino acids far apart along the chain

A

tertiary structure

91
Q

two or more chains folded together

A

quaternary structure

92
Q

two protein structures together

A

dimer

93
Q

three protein structures together

A

trimer

94
Q

four protein structures together

A

tetramer

95
Q

protein role: structure

A

keratin (nails), collagen (bone)

96
Q

protein role: communication

A

hormones

97
Q

protein role: membrane transport

A

Na-K pump

98
Q

protein role: recognition & defense

A

antibodies, clotting protein

99
Q

protein role: contraction (movement)

A

actin & myosin

100
Q

protein role: cell adhesion

A

N-cadherin

101
Q

protein role: catalysis

A

enzyme

102
Q

proteins that function as biological catalysts

A

enzymes

103
Q

nonprotein partners (iron, copper, zinc, magnesium, or calcium ions), bind to enzyme and change shape

A

cofactors

104
Q

organic cofactors derived from water-soluble vitamins (niacin, riboflavin)

A

coenzymes

105
Q

single or double carbon-nitrogen ring

A

nitrogenous base

106
Q

body’s most important energy transfer molecule

A

ATP

107
Q

nucleotides involved in energy transfer

A

guanosine triphosphate (GTP)

108
Q

synthesized from ATP

A

cyclic adenosine monophosphate (cAMP)

109
Q

DNA

A

deoxyribonucleic acid

110
Q

RNA

A

ribonucleic acid

Anatomy & Physiology I (15 decks)

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