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

chapter 2- chemistry Flashcards

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
Q

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

A

secondary

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26
Q

native conformation

A

protein in its proper shape

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27
Q

excessive heat or the wrong pH can WHAT a protein

A

denature

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28
Q

active site

A

where the enzyme has the specificity to bind to its substrate

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29
Q

cofactor

A

ion or molecule that binds to an enzyme to activate it

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30
Q

glycoprotein

A

molecule that consists of a small part carbohydrate and a large part protein

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31
Q

nucleotide nitrogenous base that is found in RNA but not DNA

A

uracil

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32
Q

WHAT serves as the copy of DNA instructions for creating the primary structure of a protein

A

messenger RNA/mRNA

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33
Q

ATP(adenosine triposphate)

A

two extra phosphate groups attached to an A base nucleotide for RNA form the high energy molecule

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34
Q

organic molecules

A

-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

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35
Q

carbon skeleton

A

chain of carbon with hydrogen

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36
Q

macromolecules

A

-small organic molecules
-involves dehydration synthesis of monomers into polymers

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37
Q

polymers

A

linkages of multiple monomers

38
Q

solution

A

uniform mixture

39
Q

colloid

A

containing dispersed proteins or other large solutes

40
Q

suspension

A

solution containing large particles that settle(ex:blood)

41
Q

carbohydrates

A

-3% of body
-starches and sugar
-catabolized for energy
-building blocks for DNA, RNA, amino acids and nutrient reserves

42
Q

monosacchride

A

-simple sugar(glucose)
-made of C6H1206
-fructose

43
Q

isomers

A

two molecules have same chemical formula but differ in shape

44
Q

disacchride

A

-sucrose(glucose + fructose)
-two covalently bonded monosaccharides
-created by dehydration synthesis
-catabolized by hydrogen

45
Q

polysaccharide

A

-3 or more monosaccharides
-storage form of glucose produced by skeletal muscle and liver cells

46
Q

lipids

A

-12-24%
-fats, oils, waxes, nonpolar
-energy storage for longer, cell membranes & cellular communication

47
Q

fatty acids

A

-hydrocarbon chain with carboxyl groups
-hydrophobic making molecule insoluble

48
Q

functional groups

A

bonding of carbon and hydrogen with other elements

49
Q

saturated and unsaturated fatty acids

A

-one or more double covalent bond
-saturated= animal source(unhealthy)
-unsaturated= plant source(healthy)

50
Q

leukotrienes

A

signal injury in cell communication

51
Q

prostaglandins

A

pain and inflammation after injury(coordinates events)

52
Q

glycerides

A

-C3H8O3 + fatty acids
-number of fatty acids bonded to glycerol group by dehydration

53
Q

a.monoglycerides
b.diglycerides
c.triglycerides

A

-make up fat deposits on animals
-energy storage
-insulation
-mechanical protection(knees and eye sockets)

54
Q

organic molecules(excess of them)

A

can be converted into triglycerides for storage via dehydration synthesis

55
Q

steriods

A

-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
Q

phospholipids

A

-diglyceride + phosphate(non-lipid)
-predominant of cell membrane

57
Q

glycolipids

A

diglyceride + carbohydrate

58
Q

micelle

A

sphere formed with hydrophilic heads oriented out toward the water and
hydrophobic tails pointed away from water

59
Q

proteins

A

-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
Q

amino acid structure

A

-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
Q

polypetide

A

chain of peptide-bonded amino acids

62
Q

primary structure

A

unique sequence of amino acids directed by DNA
* dictated by genes within DNA

63
Q

secondary structure

A

local twisting/folding of polypeptides between neighbor amino and carboxyl groups to H

64
Q

tertiary structure

A

global folding due to chemical interactions between R groups

65
Q

quaternary structure

A

aggregation of 2 more or more tertiary-folded polypeptide chains (for multi-subunit proteins)

66
Q

globular

A

compact, rounded, soluble

67
Q

fibrous

A

sheets or strands, non-
soluble

68
Q

enzymes

A

-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
Q

enzyme specificity

A

unique 3D shape creates a pocket called an active site

70
Q

enzyme saturation limit

A

maximum rate of reaction, adding more substrate will increase the reaction rate until saturation

71
Q

substrate

A

a molecule that an enzyme reacts with

72
Q

enzyme saturation

A

active site full and reaction can go no faster to produce products

73
Q

enzyme regulation

A

co-factors can turn enzymes on and off and provides short term control over reaction

74
Q

coenzymes

A

non-protein organic molecules that acts as co-factor

75
Q

anabolic reaction

A

building of molecules

76
Q

conjugated proteins

A

bound to other organic molecules

77
Q

glycoproteins

A

small carbohydrate attached to large protein
ex: mucus

78
Q

proteoglycan

A

large polysaccharide linked by polypeptides
ex: “glue” in connective tissue

79
Q

nucleic acids

A

-less than 1% of body mass
-stores and processes info at molecular level
-composed of nucleotides
- 2 types: DNA & RNA

80
Q

nucleotides

A

-linked by dehydration synthesis
-3 parts:
1. pentose sugar(ribose or deoxyribose)
2. phosphate group
3. nitrogen bases

81
Q

nitrogen purine base

A

-double ring
-adenine & guanine(A,G)

82
Q

nitrogen pyrimidine base

A

-single ring
-cytosine, thymine & uracil (C,T,U)

83
Q

linear “backbone”

A

sugar of one nucleotide to
phosphate of next creating a line with the bases hanging off the side

84
Q

RNA (ribonucleic acid)

A

-protein synthesis
-single-stranded
-backbone = ribose & phosphate
- bases: A,U,G,C
- 3 types:
1.mRNA
2.rRNA
3.tRNA

85
Q

mRNA (messenger)

A

template for a protein, order of amino acids (the primary structure of a protein)

86
Q

rRNA (ribosomal)

A

forms ribosomes: organelle for protein synthesis

87
Q

tRNA (transfer)

A

carrier to bring amino acids to ribosomes

88
Q

DNA (deoxyribonucleic acid)

A

-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
Q

gene

A

specific order of one strand of DNA that encodes RNA visually encodes a protein

90
Q

high energy molecules

A

-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
Q

phosphorylation

A

bonding of phosphate group to an organic molecule

92
Q

ATP (adenosine triphosphate)

A

-adenine + ribose + 3 phosphates
-hydrolysis of a bond to 3rd phosphate releases energy

anatomy and physiology exam 1 (3 decks)

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