Chapter 2 Flashcards

1
Q

4 major elements of the body

A

O, C, H, N

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2
Q

8 lesser elements of the body

A

Ca, P, K, S, Na, Cl, Mg, Fe

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3
Q

isotope

A

atoms of an element that have different numbers of neutrons and therefore different mass numbers

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4
Q

Ion

A

an atom that has a positive or negative charge because of unequal numbers of protons and electrons

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5
Q

molecule

A

when two or more atoms share electrons

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6
Q

compound

A

a substance that contains atoms of two or more different elements

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7
Q

free radical

A

an atom or group of atoms with an paired electron in the outermost shell

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8
Q

valence shell of electrons

A

outermost shell of electrons

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9
Q

ionic bond

A

the force of attraction that holds together ions with opposite charges

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10
Q

cation

A

ion with a positive charge

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11
Q

anion

A

ion with a negative charge

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12
Q

electrolyte

A

an ionic compound that breaks apart into positive and negative ions in solution

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13
Q

covalent bond

A

two or more atoms share electrons

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14
Q

polar

A

the sharing of electrons is unequal - one atom attracts the electrons more strongly than the other

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15
Q

nonpolar

A

the sharing of electrons is equal

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16
Q

hydrogen bond

A

forms when a hydrogen atom with a partial positive charge attracts the partial negative charge of neighbouring electronegative atoms (F/O/N)

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17
Q

chemical reaction

A

occurs when new bonds form or old bonds break between atoms

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18
Q

metabolism

A

all the chemical reactions occurring in the body

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19
Q

catalyst

A

chemical compounds that speed up chemical reactions by lowering the activation energy needed for a reaction to occur.

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20
Q

anabolism/ synthesis reaction

A

when two or more atoms, ions or molecules combine to form two new and larger molecules
A + B = AB

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21
Q

catabolism/ decomposition reaction

A

split up large molecules into smaller atoms, ions or molecules
AB = A + B

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22
Q

exchange reaction

A

AB + CD = AD + BC

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23
Q

reversible reaction

A

the products can revert to the original reactants (indicated by two half arrows pointing in opposite directions) - sometimes reversible only under certain conditions
AB = A + B

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24
Q

inorganic compound

A

usually lack a carbon and are structurally simple. Can contain ionic and covalent bonds

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25
organic compounds
always contain carbon, usually contain hydrogen and always have covalent bonds
26
water
most abundance inorganic compound in all living systems
27
water as a solvent
versatile solvent because its polar covalent bonds, in which electrons are shared unequally, create positive and negative regions.
28
hydrophillic
water loving (dissolve easily)
29
hydrophobic
water fearing ( not very water soluble)
30
hydrolysis
decomposition reactions break down large molecules into smaller molecules by the addition of a water molecule
31
dehydration synthesis
when two smaller molecules join to form a larger molecule where water is a product
32
heat capacity of water
high heat capacity - water can absorb or release a large amount of heat with only a modest change in its own temperature
33
water as a lubricant
water is a major component of mucus and lubricating fluids
34
mixture
combination of elements or compounds that are physically blended together but not bound by chemical bonds
35
solution
combination of elements that are bound by chemical bonds
36
solvent
dissolves another substance
37
solute
dissolves in another substance
38
acid
dissociates not one or more hydrogen ions
39
base
dissociates into one or more hydroxide ions (OH)
40
salt
dissociates into cations and anions (not H or OH)
41
acid base balance
there is an optimum pH level for interstitial fluid that needs to be maintained for optimal functioning (7.35-7.45)
42
pH scale
solution's acidity or alkalinity is expressed on the pH scale
43
acidic solution
pH < 7
44
basic/ alkaline solution
pH > 7
45
buffer system
function to convert strong acids or bases into weak acids or bases (which change pH less drastically)
46
carbonic acid- bicarbonate buffer system
carbonic acid acts as a weak acid and bicarbonate ion acts as a weak base. This system can compensate for either excess or shortage of H+ ions.
47
carbohydrate
sugars, glycogen, starches and cellulose
48
monosaccharide
monomer of carbohydrate - contains 3-7 carbon atoms
49
disaccharide
molecule formed from combo of 2 monosaccharides
50
polysaccharides
contains tens or hundreds of monosaccharides joined through dehydration synthesis
51
glycogen
main polysaccharide in the body- made entirely of glucose monomers linked together in branching chains
52
lipid
contain carbon, hydrogen and oxygen
53
lipoproteins
lipid molecules join with hydrophilic protein molecules (to become more soluble in blood)
54
fatty acid
simplest lipid - used to synthesize triglycerides or catabolized to generate ATP
55
triglyceride
most plentiful lipid in the body- consists of a single glycerol and 3 fatty acid molecules
56
glycerol
3 carbon glycerol forms the backbone of a triglyceride
57
phospholipid
glycerol backbone and 2 fatty acid chains attached to the first 2 carbons, form many membranes
58
steroid
4 rings of carbon atoms
59
elcosanoids
lipids derived from a 20 carbon fatty acid
60
prostaglandins
subclass of elcosanoid - modify responses to hormones, contribute to inflammatory response, prevent stomach ulcers
61
leukotrienes
subclass of elcosanoid - participate in allergic and inflammatory response
62
protein
large molecules that contain carbon, hydrogen, oxygen and nitrogen - largely responsible for the structure of body tissue
63
structural function of proteins
form structural framework of various parts of body i.e. collagen in bone and other connective tissue
64
regulatory function of proteins
function as hormones that regulate various physiological processes; control growth and development; as neurotransmitters, mediate responses of nervous system
65
contractile function of proteins
allow shortening of muscle cells which produces movement i.e. actin and myosin
66
immunological function of proteins
aid responses that protect body against foreign substances and invading pathogens
67
transport function of proteins
carry vital substances throughout body
68
catalytic function of protein
act as enzymes that replace biochemical reactions i.e. salivary amylase
69
amino acid
monomers of proteins
70
peptide bond
covalent bond joining each pair of amino acids
71
dipeptide
2 amino acids combined
72
tripeptide
3 amino acids combined
73
polypeptide
4+ amino acids combined
74
primary structure
unique sequence of amino acids that are linked by covalent bonds to form a polypeptide chain
75
secondary structure
repeated twisting or folding of neighbouring amino acids in the polypeptide chain
76
tertiary structure
3D shape of a polypeptide chain determines how it will function
77
quaternary structure
the arrangement of the individual polypeptide chains relative to one another
78
denaturation
if a protein encounters an altered environment it may unravel and lose its characteristic shape
79
DNA
forms inherited genetic material inside each human cell
80
RNA
relays instructions from the genes to guide each cell's synthesis of proteins from amino acids
81
nucleotide
monomer of nucleic acid
82
nitrogenous base
Adenine, Thymine, Cytosine and Guanine
83
deoxyribose
5C sugar attaches to each base in DNA
84
double helix
DNA resembles a spiral ladder
85
ribose
5C sugar attaches to each base in RNA
86
ATP
energy currency of all living things - 3 phosphate groups attached to adenosine
87
ADP
removal of the third phosphate group from ATP
88
enzyme
highly specific, very efficient and subject to a variety of cellular controls
89
substrate
reactant molecule on which the enzyme acts
90
active site
the place on the enzyme where the substrate binds