Chapter 2 Anatomy & Physilogy

Front 1

what is chemistry

Back 1

chemistry is the science of the structures of matter

Front 2

atoms are

Back 2

atoms are building blocks of matter

Front 3

what is matter

Back 3

matter is anything that occupies space

Front 4

what is mass

Back 4

mass is the mount of matter in any object

Front 5

what is weight

Back 5

weight is the force of gravity acting on matter

Front 6

in outer space weight is_____ but mass____

Back 6

in outer space weight is close to 0 but mass remains the same as on earth

Front 7

atoms

Back 7

atoms are substances that can not be split into simples substances by ordinary means

over 115 elements (92 occur naturally)

Front 8

4 elements that from 96% of body's mass

Back 8

oxygen, carbon, hydrogen, and nitrogen

Front 9

9 less common elements

Back 9

Ca, P, K, Na, Cl, Mg, Fe, &I

Front 10

atoms are smallest...

Back 10

atoms are smalls units of matter that retain properties of an elements

Front 11

atoms consists of 3 subatomic particles

Back 11

protons +

neutotons o

electrons -

Front 12

electrons

Back 12

surround the nucleus as a cloud (electrons are designation regions of the cloud)

Front 13

electron shells

Back 13

most likely region of the elctron cloud where to find electrons

Front 14

1st shell holds

Back 14

2 electrons

Front 15

2nd shell holds

Back 15

8 electrons

Front 16

3rd shell can hold

Back 16

up to 8 electrons

Front 17

higher shells can hold

Back 17

up to 18 electrons

Front 18

number of electrons =

Back 18

# of electrons = # of protons

Front 19

each atom is electrically __

Back 19

neutral

Front 20

what is atomic number

Back 20

number of protons in the nucleus

Front 21

that is mass number

Back 21

the sum of its protons and neutrons

Front 22

mole is

Back 22

mole Is quantity of an element with a weight (in grams) = equal to that element's atomic weight

Front 23

isotopes

Back 23

atoms of an element with different numbers of neutrons & different mass numbers

Front 24

all isoptopes of an elements have same properties which are ?

Back 24

have same # if electrons( which determine its chemical properties)

Front 25

only radioactive isotopes are unstable how do they become stable ?

Back 25

they decay overtime to a more stable configuration

Front 26

what is half-life

Back 26

half life is time required for half of the radioactive atoms in a sample to decay

Front 27

what are free radicals

Back 27

atoms with an unpaired electron in is outmost shell

unstable and highly reactive

Front 28

how can free radicals become stable (2)

Back 28

by giving up electrons

taking one off another molecule ( breaking apart important body molecules)

Front 29

how are free radicals produced

Back 29

produced in your body by absorption energy in ultraviolet light in sunlight,

x-rays by breakdown of harmful substances , and during normal metabolic reactions

Front 30

how may damaged be slowed

Back 30

with antiolxidants such as vitamin C and E

Front 31

what are chemicals properties

Back 31

chemical properties are a function of the outer electron shell

Front 32

ionic bonds

Back 32

ionic bonds are formed from electrical attractions between ions of opposite charge

Front 33

covalent bonds

Back 33

covalent bonds are formed from sharing of electrons

Front 34

Hydrogen bonds

Back 34

hydrogen bonds are weak attractive forces between the positive poles from covalent hydrogen bonds and negative poles of other covalent bonds

Front 35

cation

Back 35

lose an electron

Sodium loses al electron to become Na+

Front 36

anion

Back 36

gains an electron

chlorines gains an electron to become Cl-

Front 37

ionic compounds generally exists

Back 37

exist as solids

NaCl table salt

Front 38

Polar Covalent bonds

Back 38

unequal sharing of electrons between atoms

Front 39

in a water molecule oxygen attract hydrogen electrons more ___

Back 39

in a water molecule oxygen attract hydrogen electrons more strongly

Front 40

non-polar covalent

Back 40

share the electron(s) equally no net charge

Front 41

hydrogen bonds

Back 41

only about 5 % as strong as covalent bonds

useful in establishing links between molecules

Front 42

chemicals reaction

Back 42

when new bonds form or old bonds are broken

Front 43

metabolism

Back 43

all the chemical reactions in the body

Front 44

law of conversation of mass

Back 44

total mass of reactants equals the totoal mass of the products

Front 45

ADP + P = ATP

Back 45

requires energy

Front 46

ATP=ADP + P

Back 46

releases energy

Front 47

synthesis reactions

Back 47

2 or more atoms, ions or molecules combine to form new & larger molecules

Front 48

anabolism

Back 48

all the sysntheis reactions in the bidy together

Front 49

endergonic

Back 49

require investment of energy

energy is stored in the new bonds

amino acids to from a protein molecule

Front 50

Decomposition Reactions

Back 50

large molecules are split into smaller atoms, ion or molecules

Front 51

catabolism

Back 51

all decomposition reactions occurring together in the body

Front 52

exergonic

Back 52

release energy stored in chemical bonds

Front 53

chemical reactions can be reversivle

Back 53

reactants can be products or products can revert to the original reactants

Front 54

Chemicals reactions involve___

Back 54

chemicals reactions involve energy changes

Front 55

law or conservation of energy

Back 55

energy can neither be created nor destroyed - just converted from one form to another

Front 56

kinetic energy

Back 56

energy of motion

Front 57

potential energy

Back 57

stored energy

Front 58

what is chemical energy

Back 58

chemical energy is potential energy stored in the bonds of molecules

digestion of food releases chemical energy so that It can be converted to hear or mechanical energy

Front 59

activation energy

Back 59

energy needed to begin a reaction

Front 60

catalsyst do what

Back 60

catalysts speed up chemical reaction by lowering the activation energy

Front 61

normal body temperatures and concentrations are too ___ to allow chemical reactions to occur

Back 61

are too low to allow chemical reactions to occur

Front 62

enzymes orient the colliding particles properly...

Back 62

so that they touch at the spots that make the reaction happen

Front 63

enzymes are ___ by reactions and

Back 63

enzymes are unchanged by the reaction, and can be used repeatedly in similar reations

Front 64

most of the chemicals in the body are___

Back 64

compounds (2 or more elements)

Front 65

inorganic compounds

Back 65

usually lack carbon & are structurally simple

water, oxygen, Co2, salts, acids, and bases`

Front 66

organic compounds

Back 66

contain carbon, hyrdrogen, and usually oxygen

always have covalent bond

Front 67

most compunds exist in a nature as

Back 67

mixtures

Front 68

what is a mixture

Back 68

a combination of elements or compounds that are physically blended but not joined by bonds --air

Front 69

solutions

Back 69

when solutes dissolved in a solvent

Front 70

colloids

Back 70

when solutes are mixed in a solvent

particles are larger so does not look clear (milk)

particles do not settle out of solution

Front 71

suspensions

Back 71

have larger solutes mixed in a solvent

particles settle out of solution because of size blood

Front 72

water

Back 72

most important inorganic compound in living systems

medium of nearly all chemical reaction

Front 73

5 things about water

Back 73

makes excellent solvent for ionic or polar substances

ions become electrolytes as they can conduct a current

gives water molecules cohesion (surface tension

allowes water to moderate temperature change

major component of lubricating fluids`

Front 74

most versatile solvent

Back 74

water

Front 75

water has ____ bonds

Back 75

polar covalent

Front 76

water's shape allows__

Back 76

waters shape allows each water molecule to interact with adjacent ions/molecules

Front 77

H20 + NaCl

Back 77

oxygen attracts sodium

sodium & chloride separate as ionic bonds are broken

hydration spheres surround each ion a posibilty of bonds being reformed

Front 78

water____ many substancess

Back 78

water dissolves or suspends many substances

Front 79

non polar moleucles

Back 79

do not have positive or negative poles

lack or few covalent bonds

Front 80

when non polar covalent bonds are exposed to water

Back 80

hydration spheres do NOT form and the molecules do NOT dissolve

Front 81

hydrophibic

Back 81

molecules that do not readily react with water

ex)fats and oils

Front 82

ph 0-6

Back 82

acidic

Front 83

ph 8-14

Back 83

alkaline

basic

Front 84

ph of 1 ___ timex more H+ than pH of 2

Back 84

ph of 1 (10 times more H+ than ph of 2)

Front 85

ph of ______ is maintained in blood

Back 85

7.35-7.45

Front 86

water in chemical reactions

Back 86

participates as a product or reactant in certain reactions in the body

Front 87

hydrolysis reactions

Back 87

water is added to separate it into 2 smaller molecules

Front 88

dehydration synthesis reaction

Back 88

two smaller molecules are joined to form a larger molecules releasing a water molecule

Front 89

organic compounds

Back 89

always contain carbon and hydrogen

usually large, unique molecules with complex functions

make up 40% of body mass

Front 90

properties of carbon atoms

Back 90

from bonds with other carbon atoms produce large molecules

with many different shapes (rings, straight, or branched chains)

some large molecules may not dissolve in water

Front 91

many functional groups cab attach to carbon skeleton

Back 91

ester, amino, carboxyl, phosphate groups

Front 92

macromolecules

Back 92

very large molecules (polymers if all monomers subunits are similar)

Front 93

isomers

Back 93

have same molecular but different structures

glucose & fructose are both C6H1206

Front 94

sterioisomers

Back 94

isomeric molecules that have the same molecular formula and sequence of bonded structure , but different 3-D orientations pf their atoms in space

Front 95

carbohydrates (watered carbon)

Back 95

diverse group of substances formed from C,H, and O

main function is source of energy for ATP formation

forms only 1-3 % % of total body weight`

Front 96

glycogen

Back 96

storage in liver and muscle tissue

Front 97

sugar bulding bloacks of DNA & RNA

Back 97

carbohydrates

Front 98

monosaccharides

Back 98

simple sugars

contains 3-7 carbon atoms

we can absord only 3 simple sugars without further digestion in our small intestine

Front 99

3 examples of monosaccharides

Back 99

glucose found in syrup or honey

fructose found in fruit

galactose found in dairy products

Front 100

Disaccharides

Back 100

formed by combining 2 monosaccharaides by dehydration synthesis (releasing water molecule)

Front 101

sucrose =

Back 101

glucose + fructose (both isomers)

Front 102

maltose =

Back 102

glucose + glucose

Front 103

lactose=

Back 103

glucose & galactose

Front 104

Polysaccharides

Back 104

contains 10 or 100's of monosaccharaides joined by dehydration synthesis to from starches

Front 105

in animals glycogen

Back 105

glycogen is a chain of hundreds of glucose molecules

found in liver & skeletal muscle

when blood sugar level drops, liver hydrolyzes glycogen to create and releae glucose into the bloodn

Front 106

in planst cellulose is

Back 106

large carbohydrates molecules used for energy storage

(rice, potatoes, grains)

Front 107

lipids

Back 107

fats

formed C , H, & O

18-25% of body mass`

Front 108

examples of lipids

Back 108

fatty acids, glycerides, steroids, phospholipids, glcyolipids, eiscosanoids, liproprotains, and some vitmainds

Front 109

hydrophobic of lipids

Back 109

fewer polar bonds because of fewer oxygen atoms

insoluble in polar solvents like water

Front 110

lipoproteins

Back 110

combines with proteins for transport in bloof

Front 111

triglycerides

Back 111

neutrals fats composed of a single glycerol molecule and 3 fatty acid molecule

very concentrated from of energy

source of insulation preventing heat loss

source of protection by cushioning delicate organs

3-carbon glycerol ml\molecule is the backbone

Front 112

triglyceride structure

Back 112

3 fatty acids & one glycerol molecule

fatty acids attached by dehydration synthesis

Front 113

saturation of tryglyerides

Back 113

determined by number of single or double covalent bonds

saturated fats contain single covalent bonds and ae covered with hydrogen atoms

Front 114

monosaturated

Back 114

are not complerlt covered with hydrogen-- olive, canpla, and peanut oils

Front 115

polysaturated fats

Back 115

contain even less hydrogen atoms-- safflower and corn oils along with oils from fatty fish

Front 116

phosphliids composition

Back 116

a polar head

a phosphate group (PO4)& glycerol molecule

can form hydrogen bonds with water

2 non polar fatty acid tails

interact only with lipids

Front 117

amphipathic

Back 117

molecules with polar & nonpolar parts

Front 118

(phospholipid) composition of cell membrane

Back 118

double layer of phospholipids with tails in center

Front 119

how are steroids formed

Back 119

formed from 4 rings of carbon atoms joined together

Front 120

why are steroids classified as sterols

Back 120

classified as sterols because they have alcohol group attached to one or more of the rings

Front 121

cholesterol found in ____

Back 121

found in animal cell membranes

starting material for synthesis of other steroids

Front 122

cholesterol derivatives include

Back 122

sex hormones & adrenal cortex hormones

bile salts

vitamin D

Front 123

eicosanoids

Back 123

lipid type derived from a fatty acids called arachidonic acid (from food sources only)

Front 124

prostaglandins= wide variety of functions (6)

Back 124

modify responses to hormones

contribute to inflammatory response

prevent stomach ulcers

dilate airways

regulate body temperature

influence formation of blood clots

Front 125

leukotrienes=

Back 125

allergy & inflammatory response

Front 126

protein (polymer)

Back 126

18-20% of body weight

contain carbon, hydrogen, oxygen, and nitrogen

constructed from combinations of 20 different amino acids

Front 127

how are dipeptides formed from

Back 127

2 amino acids joined by a covalent bond called a peptide bond

Front 128

peptides formed

Back 128

from a few amino acids (under 10)

Front 129

polypeptide chains formed

Back 129

from 10-100 (but can be as high as 200 amino acids (but can be as high as 2000 amino acids)

Front 130

levels of structural organization

Back 130

primary, secondary, tertiary, (and quaternary)

shape of the protein influences its ability to from bonds`

Front 131

amino acid (monomer structure)

Back 131

central carbon atom

amino group (NH2)

Carboxyl group (COOH)

Side Chains (R groups) vary between amino acidds

Front 132

dipeptides formed from

Back 132

2 amino acids joined by a covalent bond called a peptide bond- dehydration synthesis

Front 133

polypeptides typically formed

Back 133

from 10-100 amino acids

Front 134

proteins contin

Back 134

over 100 amino acids to form a functional until form polypeptides

Front 135

primary is

Back 135

unique sequence of amino acids

Front 136

secondary

Back 136

is alpha helix or pleated sheet folding

Front 137

tertiary is

Back 137

3-D shape of polypeptide chain

Front 138

Quaternary is

Back 138

relationship of multiple of multiple of polypeptide chains

Front 139

Disulfide bridges

Back 139

stabilize the tertiary structure of protein molecules

Front 140

____ between sulfhydryl groups of 2 cysteine amino acids

Back 140

covalent bonds between sulfhydryl groups of 2 cysteine amino acids

Front 141

fibrous proteins

Back 141

arranged in sheets or strands

Front 142

Globular Proteins

Back 142

compact, rounded and quite hydrophillic

Front 143

____dictates function

Back 143

Protein structure dictates function

Front 144

7 protein functions

Back 144

1. structural support

2. Metabolism of cell

3. Defense

4. Transport

5. Movement

6. Homeostasis

7. Plasma Membrane

Front 145

structural support

Back 145

collagen, keratine, etc

Front 146

metabolism of cell

Back 146

enzymes (similar enzymes from different organs are called isoenzymes)

Front 147

defense

Back 147

antibodies (IG's) & waterproofing of skin, hair and nails

Front 148

transport

Back 148

many hydrophobic substances are bound to transport proteins (globulins) for transport

Front 149

movement

Back 149

actin/myosin contract muscles

Front 150

homeostasis

Back 150

non steroidal hormones

Front 151

plasma membrane-

Back 151

glycoproteins for self recognition, and transmembraneous channels for selective permeability

Front 152

function of protein depends on

Back 152

depends on its ability to recognize and bind to some other molecle

this determined by its "folded" 3-D shape

Front 153

hostile enviroments such as heat, acid, or salts will____

Back 153

change a proteins 3-D shape and destroy its ability to function

Front 154

enzymes

Back 154

enzymes are protein molecules that act as catalysts

Front 155

some enzyme=

Back 155

apoenzyme + cofactor

Front 156

apoenzymes

Back 156

are the protein portion

Front 157

cofactors

Back 157

are non protein portion

Front 158

cofactors may be

Back 158

metal ion (iron, zinc, magnesium, or calcium)

may be organic molecules derived from a vitamin

Front 159

enzymes usually end in suffux ___ and are named for the ___

Back 159

enzymes usually end in suffix -ase and are named for the types of chemical reactions they catalyze

Front 160

isoenzymes

Back 160

same function different organ

Front 161

bonds are made or broken

Back 161

bonds are made or broken when atoms, ions or molecules collide

Front 162

enzymes speed up reactions by

Back 162

enzymes speed up reaction by properly orienting colliding molecules, reducing activation energy

Front 163

1000+ known enymes ____ to 10 billions that in beaker

Back 163

1000+ known enzymes speed up metabolic reactions to 10 billion times that in beaker

Front 164

cofactor

Back 164

non organic metal ion

Front 165

coenzyme

Back 165

organic vitamin

Front 166

enzyme functionality (highly specific )

Back 166

acts on only on substrate

speed up only one reaction

Front 167

active site:

Back 167

exact fit vs induced fit

Front 168

enzyme functionality (very efficient)

Back 168

speed up reaction up to 10 billion times faster

Front 169

enzyme functionality (under cellular control)

Back 169

rate of synthesis of enzyme

inhibitory substances

inactive forms of enzyme

Front 170

DNA (polymer) structure

Back 170

huge molecules containing C,H,O,N and phosphorus

Front 171

a molecule of DNA is

Back 171

a chain of nucleotideses

Front 172

Nucleotide=

Back 172

nitrogenous base (A-G-T-C) + pentose sugar+ phosphate group

Front 173

each doube helix stand serves as

Back 173

template for new DNA

Front 174

RNA differe from DNA

Back 174

single stranded

ribose sugar not deoxyribose sugar

uracil nitrogenous bases replaces thymine

Front 175

types of RNA within the cell, each with a specific function

Back 175

messenger RNA

Ribosomal RNA

Transfer RNA

Front 176

ATP

Back 176

temporary molecular storage of energy as it is being transferred from exergonic catabolic reactions to cellular activities