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
bond formed with Hydrogen; mostly within water molecules
hydrogen bonds
24
weak, brief attractions between neutral atoms
Van der Waals forces
25
molecules with identical molecular formulas but different arrangement of their atoms
isomers
26
substances physically blended, but not chemically combined
mixture
27
the ability for water to stick to other molecules
adhesion
28
the ability for water to stick to itself; causes surface tension
cohesion
29
ability to dissolve other chemicals
solvency
30
the universal solvent
water
31
particles in water that cannot be seen
solution
32
particles stay suspended, but do not separate out on standing; cloudy/translucent
colloid
33
particles are too large that it separates on standing; cloudy/opaque
suspension
34
water's ability to participate in chemical reactions
chemical reactivity
35
helps water stabilize internal temperature of the body
thermal stability
36
of moles of solute per liter in a solution
molarity
37
proton donor (releases H+ ions)
acid
38
proton acceptor (accepts H+ ions)
base
39
pH 7.0
neutral
40
pH > 7.0
basic
41
pH< 7.0
acidic
42
resists change in pH
buffers
43
What is the pH of blood?
7.35-7.45
44
process in which covalent or ionic bond formed or broken
chemical reactions
45
large molecule breaks down into two or more smaller ones
decomposition
46
two or more small molecules combine to form a larger
synthesis reaction
47
two molecules exchange atoms or groups of atoms
exchange reaction
48
reaction that can go either way
reversible reaction
49
reactions that break covalent bonds, exergonic, decomposition
catabolism
50
energy releasing reactions
exergonic
51
reactions that store energy, endergonic, synthesis reaction; REQUIRES energy input
anabolism
52
energy using reactions
endergonic
53
a molecule that gives up electrons; releases energy
oxidation
54
electron donor
reducing agent
55
a molecule that gains electrons; gains energy
reduction
56
electron acceptor
oxidizing agent
57
study of compounds containing carbon
organic chemistry
58
four categories of carbon compounds
carbohydrates, lipids, proteins, nucleic acids
59
small molecules that can react with other molecules to form large/complex molecules
monomers
60
molecules made of repetitive series of identical similar subunits (monomers)
polymers
61
determines properties of organic molecules
functional groups
62
joining monomers to form a polymer; formed by dehydration synthesis
polymerization
63
splitting polymer (LYSIS) by adding water molecules
hydrolysis
64
hydrophilic organic molecule
carbohydrates
65
glucose, galactose, fructose
monosaccharide
66
sucrose, lactose, maltose (made of two monosaccharides)
disaccharides
67
short chains of monosaccharides (3 or more)
oligosaccharides
68
long chains of monosaccharides (50 or more)
polysaccharides
69
energy storage polysaccharide in human tissue
glycogen
70
energy storage polysaccharide in plants
starch
71
structural molecule of plants cell walls
cellulose
72
hydrophobic organic molecules
lipids
73
no H+ can be added (solid at room temperature)
saturated fatty acids
74
has double bond (liquid at room temperature)
unsaturated fatty acids
75
resists enzymatic breakdown, circulates longer, deposits in arteries
trans-fatty acids
76
found naturally in food; beneficial
cis-fatty acids
77
three fatty acids covalently bonded to glycerol; bond formed by dehydration synthesis
triglycerides
78
solid triglyceride at room temperature
fats
79
liquid triglyceride at room temperature
oils
80
one fatty acid replaced by a phosphate group
phospholipid
81
both water fearing and loving
amphiphilic
82
derived from arachidonic acid; hormone like chemical signals between cells
eicosanoids
83
good proteins, lower ratio of lipids to proteins
high density lipoproteins
84
bad proteins, high ratio of lipid to proteins
low density lipoproteins
85
polymer of amino acids
proteins
86
amino acids have a central carbon with one of these attachments
amino, carboxyl, radical
87
loss of conformation and function of a protein
denaturation
88
linear sequence of amino acids
primary structure
89
pattern caused by interaction in nearby amino acids, helix or pleated sheet
secondary structure
90
connections between amino acids far apart along the chain
tertiary structure
91
two or more chains folded together
quaternary structure
92
two protein structures together
dimer
93
three protein structures together
trimer
94
four protein structures together
tetramer
95
protein role: structure
keratin (nails), collagen (bone)
96
protein role: communication
hormones
97
protein role: membrane transport
Na-K pump
98
protein role: recognition & defense
antibodies, clotting protein
99
protein role: contraction (movement)
actin & myosin
100
protein role: cell adhesion
N-cadherin
101
protein role: catalysis
enzyme
102
proteins that function as biological catalysts
enzymes
103
nonprotein partners (iron, copper, zinc, magnesium, or calcium ions), bind to enzyme and change shape
cofactors
104
organic cofactors derived from water-soluble vitamins (niacin, riboflavin)
coenzymes
105
single or double carbon-nitrogen ring
nitrogenous base
106
body's most important energy transfer molecule
ATP
107
nucleotides involved in energy transfer
guanosine triphosphate (GTP)
108
synthesized from ATP
cyclic adenosine monophosphate (cAMP)
109
DNA
deoxyribonucleic acid
110
RNA
ribonucleic acid