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anatomy and physiology unit 1 > chapter 2- chemistry > Flashcards

chapter 2- chemistry Flashcards

(92 cards)

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1
Q

three states of matter are liquid, solid, and WHAT

A

gas

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2
Q

electrical energy

A

the energy of the movement of charged particles

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3
Q

atomic number

A

determined by the number of protons it has

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4
Q

atomic number - atomic mass

A

to figure out how many neutrons a element has

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5
Q

isotopes

A

atoms that have the same atomic number but different masses

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6
Q

half-life

A

the time necessary for half a given amount of a radioisotope to decay

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7
Q

magnesium has an atomic # of 12, how many valence electrons

A

2 (12 electrons hat fills the valence shell 2-8-2

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8
Q

why do inert atoms not contribute to the formation of molecules?

A

they have full valence shells

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9
Q

anion

A

an atom with more electrons than protons

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10
Q

non-polar single covalent bond

A

type of chemical bond where two atoms share one pair of electrons equally

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11
Q

for hydrogen bonds to be created, there must first be molecules that
have WHAT covalent bonds between hydrogen and another atom

A

polar

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12
Q

catabolism

A

decomposition reactions of the body

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13
Q

An enzyme is a biological WHAT substance that facilitates a
reaction without becoming part of the reaction

A

catalyst

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14
Q

hydrophobic

A

molecules that don’t dissociate in water to create a solution

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15
Q

base

A

substance that dissociates to release cations and hydroxide ions

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16
Q

colloid

A

term for a solution that contains large molecules

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17
Q

A disaccharide is formed by the WHAT synthesis of two WHAT

A

dehydration and monosaccharides

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18
Q

unsaturated fatty acids

A

contain one or more double covalent bonds

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19
Q

prostaglandins are an example of lipids that are derived from arachidonic
acid and belong to the WHAT group of lipids

A

eicosanoid

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20
Q

glycolipid

A

a diglyceride with a carbohydrate group

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21
Q

steriods

A

the lipid group that is based on the carbon ring structures

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22
Q

due to the bipolar nature of phospholipids, they will spontaneously adopt a
WHAT structure, with the heads pointing out and the tails pointing in, when placed in water

A

micelle

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23
Q

peptide bond

A

covalent bonding between the amino group of one amino acid and the carboxyl group of another form

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24
Q

R group amino acids

A

have a common core structure, but they differ from each other

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25
the local folding and twisting that occurs because of H-bonding between nearby amino acids form the helices and sheets of the WHAT structure of a protein
secondary
26
native conformation
protein in its proper shape
27
excessive heat or the wrong pH can WHAT a protein
denature
28
active site
where the enzyme has the specificity to bind to its substrate
29
cofactor
ion or molecule that binds to an enzyme to activate it
30
glycoprotein
molecule that consists of a small part carbohydrate and a large part protein
31
nucleotide nitrogenous base that is found in RNA but not DNA
uracil
32
WHAT serves as the copy of DNA instructions for creating the primary structure of a protein
messenger RNA/mRNA
33
ATP(adenosine triposphate)
two extra phosphate groups attached to an A base nucleotide for RNA form the high energy molecule
34
organic molecules
-carbon-based molecules with hydrogen(minimum) and oxygen -produced by living things -allows the formation of large molecules with other molecules -either solid or solutions
35
carbon skeleton
chain of carbon with hydrogen
36
macromolecules
-small organic molecules -involves dehydration synthesis of monomers into polymers
37
polymers
linkages of multiple monomers
38
solution
uniform mixture
39
colloid
containing dispersed proteins or other large solutes
40
suspension
solution containing large particles that settle(ex:blood)
41
carbohydrates
-3% of body -starches and sugar -catabolized for energy -building blocks for DNA, RNA, amino acids and nutrient reserves
42
monosacchride
-simple sugar(glucose) -made of C6H1206 -fructose
43
isomers
two molecules have same chemical formula but differ in shape
44
disacchride
-sucrose(glucose + fructose) -two covalently bonded monosaccharides -created by dehydration synthesis -catabolized by hydrogen
45
polysaccharide
-3 or more monosaccharides -storage form of glucose produced by skeletal muscle and liver cells
46
lipids
-12-24% -fats, oils, waxes, nonpolar -energy storage for longer, cell membranes & cellular communication
47
fatty acids
-hydrocarbon chain with carboxyl groups -hydrophobic making molecule insoluble
48
functional groups
bonding of carbon and hydrogen with other elements
49
saturated and unsaturated fatty acids
-one or more double covalent bond -saturated= animal source(unhealthy) -unsaturated= plant source(healthy)
50
leukotrienes
signal injury in cell communication
51
prostaglandins
pain and inflammation after injury(coordinates events)
52
glycerides
-C3H8O3 + fatty acids -number of fatty acids bonded to glycerol group by dehydration
53
a.monoglycerides b.diglycerides c.triglycerides
-make up fat deposits on animals -energy storage -insulation -mechanical protection(knees and eye sockets)
54
organic molecules(excess of them)
can be converted into triglycerides for storage via dehydration synthesis
55
steriods
-ex: cholesterol, estrogen, & testosterone -important for cell membrane formation & maintenance -cell division and osmotic stability of cell -tissue metabolism & mineral balance -regulation of sexual function -processing of dietary fats
56
phospholipids
-diglyceride + phosphate(non-lipid) -predominant of cell membrane
57
glycolipids
diglyceride + carbohydrate
58
micelle
sphere formed with hydrophilic heads oriented out toward the water and hydrophobic tails pointed away from water
59
proteins
-20% of body mass -essential to cell structure and function -from amino acids that become polypeptides that are folded into proper native conformation a.support b.movement c.transport d.buffering e.coordination & control f.defense g.metabolic activity and regulation
60
amino acid structure
-central carbon -carboxyl groups -amino acid groups -R group -20 different amino acids -some charged -some hydrophilic -some hydrophobic -some make disulfide bonds * resulting bond = peptide bond
61
polypetide
chain of peptide-bonded amino acids
62
primary structure
unique sequence of amino acids directed by DNA * dictated by genes within DNA
63
secondary structure
local twisting/folding of polypeptides between neighbor amino and carboxyl groups to H
64
tertiary structure
global folding due to chemical interactions between R groups
65
quaternary structure
aggregation of 2 more or more tertiary-folded polypeptide chains (for multi-subunit proteins)
66
globular
compact, rounded, soluble
67
fibrous
sheets or strands, non- soluble
68
enzymes
-abundant protein in the body -biological catalyst, catalytic protein used metabolism of living cells -speed up reactions by lowering activation energy, orient molecules to favor reaction without heat or pressure
69
enzyme specificity
unique 3D shape creates a pocket called an active site
70
enzyme saturation limit
maximum rate of reaction, adding more substrate will increase the reaction rate until saturation
71
substrate
a molecule that an enzyme reacts with
72
enzyme saturation
active site full and reaction can go no faster to produce products
73
enzyme regulation
co-factors can turn enzymes on and off and provides short term control over reaction
74
coenzymes
non-protein organic molecules that acts as co-factor
75
anabolic reaction
building of molecules
76
conjugated proteins
bound to other organic molecules
77
glycoproteins
small carbohydrate attached to large protein ex: mucus
78
proteoglycan
large polysaccharide linked by polypeptides ex: "glue" in connective tissue
79
nucleic acids
-less than 1% of body mass -stores and processes info at molecular level -composed of nucleotides - 2 types: DNA & RNA
80
nucleotides
-linked by dehydration synthesis -3 parts: 1. pentose sugar(ribose or deoxyribose) 2. phosphate group 3. nitrogen bases
81
nitrogen purine base
-double ring -adenine & guanine(A,G)
82
nitrogen pyrimidine base
-single ring -cytosine, thymine & uracil (C,T,U)
83
linear "backbone"
sugar of one nucleotide to phosphate of next creating a line with the bases hanging off the side
84
RNA (ribonucleic acid)
-protein synthesis -single-stranded -backbone = ribose & phosphate - bases: A,U,G,C - 3 types: 1.mRNA 2.rRNA 3.tRNA
85
mRNA (messenger)
template for a protein, order of amino acids (the primary structure of a protein)
86
rRNA (ribosomal)
forms ribosomes: organelle for protein synthesis
87
tRNA (transfer)
carrier to bring amino acids to ribosomes
88
DNA (deoxyribonucleic acid)
-double helix -contains genes -backbone = alternating deoxyribose sugar & phosphate -order of nucleotides in DNA is the info. copied into mRNA form so it can assemble the primary structure of a protein -bases: A,T,C,G
89
gene
specific order of one strand of DNA that encodes RNA visually encodes a protein
90
high energy molecules
-used to hold chemical bond energy from food molecules in an easy-to-use form -involves phosphorylation -phosphate groups negative charge -when cell has extra energy, phosphate is bonded to ADP(low energy form) to store energy as ATP(high energy form)
91
phosphorylation
bonding of phosphate group to an organic molecule
92
ATP (adenosine triphosphate)
-adenine + ribose + 3 phosphates -hydrolysis of a bond to 3rd phosphate releases energy

anatomy and physiology unit 1 (3 decks)

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