Matc, A&p I, Elise, Ch 1&2 Test Q

Front 1

anatomy

Back 1

study of structure

Front 2

physiology

Back 2

study of function

Front 3

atom

Back 3

smallest particles with unique chemical identities (ex. elements)

Front 4

molecule

Back 4

chemical particles composed of two or more atoms united by a covalent bond

Front 5

compound

Back 5

a molecule with 2 or more different elements (ex. carbon dioxide)

Front 6

macromolecules

Back 6

any molecule of a large size
(ex. proteins, fats, DNA)

Front 7

organelle

Back 7

microscopic structures in a cell carrying out individual functions
(ex. mitochondria, lysosomes)

Front 8

cell

Back 8

smallest subdivision of a tissue considered to be alive; enclosed in a plasma membrane and usually has a nucleus

Front 9

tissue

Back 9

mass of similar cells and cell products forming a discrete region of an organ and performing a specific function
(ex. connective, muscular, nervous)

Front 10

organ

Back 10

structure composed of at least two different tissue types working together to carry out a particular function; have recognizable boundaries

Front 11

organ system

Back 11

group of organs with a unique collective function, humans have 11
(ex. skeletal, digestive)

Front 12

organism

Back 12

single complete individual

Front 13

biological criteria of life

Back 13

life is a collection of properties distinguishing living from non-living things; organization, cellular, composition, metabolism & excretion, responsiveness & movement, homeostasis, development, reproduction, evolution

Front 14

homeostasis

Back 14

internal conditions in the body remain relative stability even when external conditions vary greatly; loss of homeostatic control leads to illness or death

Front 15

dynamic equilibrium

Back 15

balanced change where there is a specific set point (average value) and conditions fluctuate around it (internal conditions not constant but fluctuate w/in a limited range)

Front 16

what are the 3 basic components of homeostasis?

Back 16

receptor= structure sensing change in the body; integrating or control center= mechanism processing info, relating it to other available info, making a decision about desired response; effector= structure carrying out response restoring homeostasis

Front 17

give an example of homeostasis

Back 17

body temperature's "thermostat" kicks in; nerve cells in brain monitoring temp are triggered and heat-losing or heat-producing mechanisms kick in; vasodilation (sweating)=heat-losing; vasoconstriction (shivering)= heat producing

Front 18

negative feedback

Back 18

process in which the body senses a change and activates mechanisms to REVERSE it; uses dynamic equilibrium (receptor, integrating center, effector) to restore homeostasis

Front 19

positive feedback

Back 19

a self-amplifying cycle in which a physiological change leads to an even greater change in the SAME DIRECTION (rather than correcting) producing rapid change and disrupting homeostasis

Front 20

give an example of positive feedback that is useful

Back 20

childbirth

Front 21

element

Back 21

simplest form of matter having unique chemical properties

Front 22

how many naturally occurring elements are there?

Back 22

91

Front 23

what are the 4 most abundant elements?

Back 23

O - Oxygen
C - Carbon
H - Hydrogen
N - Nitrogen

Front 24

what are 8 lesser elements?

Back 24

Ca - Calcium
P - Phosphorus
S - Sulfur
K - Potassium
Na - Sodium
Cl - Chlorine
Mg - Magnesium
Fe - Iron

Front 25

what are 4 trace elements?

Back 25

Se - Selenium
Cu - Copper
Zn - Zinc
I - Iodine

Front 26

atom

Back 26

smallest particles with unique chemical identities, composed of protons (p+), neutrons (n) and electrons (e-)
(ex. elements)

Front 27

proton

Back 27

positive charge, 1amu, located in nucleus
(p + n = atomic mass)

Front 28

neutron

Back 28

no charge, 1amu, located in nucleus
(p + n = atomic mass)

Front 29

electron

Back 29

negative charge, very low mass, located in electron shells surrounding the nucleus (outside)
(p+ = e- or same number in each atom)

Front 30

atomic number

Back 30

number of protons in an element

Front 31

electron shells

Back 31

located outside nucleus of atom, where electrons are located,
first shell holds 2 electrons
each subsequent shell holds 8 max (octet rule)

Front 32

valence electron shell

Back 32

outermost electron shell, determines chemical bonding properties of an atom
(wants to have 8 so gives or takes electrons to achieve octet rule, gaining a positive or negative charge in the process)

Front 33

isotopes

Back 33

same elements with differing amounts of neutrons and therefore different masses
(but same atomic number so same number of protons)

Front 34

structural isomers

Back 34

molecules with the same ratio of atoms but different arrangement of atoms
(identical molecular formula, different arrangement)

Front 35

ion

Back 35

charged particles with unequal numbers of protons and electrons; elements with 1-3 valence electrons tend to give them up (e- charge), elements with 4-7 tend to take them (e+ charge)

Front 36

anion

Back 36

loses electron so acquires e+ charge

Front 37

cation

Back 37

gains electron so acquires e- charge

Front 38

ionic bond

Back 38

attraction of cation to anion, 1 gives and 1 takes
(ex. opposite charges attract to one another and follow each other through the body)

Front 39

electrolytes

Back 39

salts ionizing in water to form solutions capable of conducting an electric current

Front 40

why are electrolytes important?

Back 40

chemical reactivity, osmotic effects (water content and distribution in body), electrical effects (nerve and muscle functioning); imbalances can cause cramps, brittle bones, coma, cardiac arrest

Front 41

free radicals

Back 41

chemical particles with an odd number of electrons; trigger chain reactions by trying to steal electrons which destroy molecules and cause tissue damage

Front 42

antioxidants

Back 42

chemical neutralizing free radicals by donating electrons; obtained in diet as Vitamins E & C, selenium, and B carotine

Front 43

covalent bond

Back 43

formed by sharing an electron or 2 or more valence electrons; strongest bond (the electrons shared swarm around both nuclei in a dumbell shaped cloud)

Front 44

single covalent bond

Back 44

sharing of a single pair of electrons, symbolized by a single line between atomic symbols (H-H)

Front 45

double covalent bond

Back 45

sharing of 2 pairs of electrons, symbolized by two lines between atomic symbols (O=C=O)

Front 46

non-polar covalent bond

Back 46

shared electrons spend approximately equal time around each nucleus
(strongest of all covalent bonds)

Front 47

polar covalent bonds

Back 47

shared electrons spend significantly more time orbiting one nucleus than the other (unequal); they lend negative charge to the region they spend the most time

Front 48

how stable are ionic bonds?

Back 48

ionic bonds break in the presence of water because they are more attracted to water than they are each other

Front 49

how are ionic bonds used in the body?

Back 49

cations and anions are loosely attracted to each other and follow each other through the body; their attraction maintains the excitability of muscle and nerve cells; electrolytes are ionized salts producing electrical charges

Front 50

how are covalent bonds used in the body?

Back 50

when 2 hydrogen form a covalent bond with oxygen a water molecule is formed (weak hydrogen bonds hold water molecules together); formed between regions of same molecules, especially large molecules such as protein and DNA

Front 51

energy

Back 51

the capacity to do work

Front 52

potential energy

Back 52

contained in an object but not doing work at the time

Front 53

kinetic energy

Back 53

energy of motion (doing work)

Front 54

how can a sugar molecule have both kinetic and potential energy?

Back 54

it has chemical energy stored as potential energy and chemical reactions release this energy and make it available for work (kinetic)

Front 55

metabolism

Back 55

all chemical reactions in the body

Front 56

catabolism

Back 56

consists of energy-releasing decomposition reactions
AB=> A + B

Front 57

decomposition reactions

Back 57

the breaking of covalent bonds to produce smaller molecules from larger molecules, the released energy can be used for physiological work
AB=> A + B
(ex. hydrolysis)

Front 58

anabolism

Back 58

consists of energy-storing synthesis reactions
A + B => AB

Front 59

synthesis reactions

Back 59

require an energy input (ENDERGONIC); driven by catabolic energy released (so inseparable)
A + B => AB
(ex. hydration)

Front 60

exchange reaction

Back 60

two molecules exchange atoms or groups of atoms
AB + CD => AC + BD

Front 61

reversible reaction

Back 61

can go in either direction under different circumstances (law of MASS ACTION)

Front 62

law of mass action

Back 62

reversible reactions proceed from the side with the greater quantity of reactancts to the side with the lesser quantity of reactants

Front 63

reaction rates

Back 63

the basis for all chemical reactions are molecular motion and collisions (molecules in constant motion and reactions occur when mutually reactive molecules collide with sufficient force and right orientation)

Front 64

what are the 3 factors effecting reaction rates?

Back 64

concentration of reactants (more=increases); temperature (heat increases); catalysts (increases)

Front 65

catalysts

Back 65

temporarily bind with reactants holding them in a favorable position to react w/ one another, may change the shapes of the reactants making them more likely to react w/ one another (reduces the element of chance and speeds up the reaction) (ex. enzymes)

Front 66

acid

Back 66

a proton donor (H+); chemical releasing protons into a solution or water

Front 67

salt

Back 67

a dietary mineral composed primarily of sodium chloride; essential for animal life
(ex. sea salt, iodized salt)

Front 68

range of pH scale

Back 68

0-14; 7 neutral
below 7 = acidic
above 7 = base (alkaline)
(lower pH = more hydrogen ions and more acidic)

Front 69

pH scale

Back 69

a change of 1 whole number represents a 10-fold change
(ex. pH 4 is ten x as acidic as pH 5; and 1000 x as acidic as pH 7)

Front 70

what is the pH of blood?

Back 70

ranges from pH 3.35 - 4.45

Front 71

what is the pH of water?

Back 71

7, chemically neutral

Front 72

define polar

Back 72

electrons shared unequally and lend their e- charge (negative) to the region where they spend the most time

Front 73

what is the structure of water?

Back 73

atoms are joined by polar covalent bonds; molecule is V shaped with a 105' bond angle (molecule as whole polar w/ a slight negative charge on the oxygen and a slight positive charge on each hydrogen)

Front 74

hydrogen bond

Back 74

weak attractions between a slightly positive hydrogen atom in one molecule and a slightly negative oxygen (or nitrogen) atom in another (water molecules are weakly attracted to each other through hydrogen bonds)

Front 75

what are the 5 properties of water that support life?

Back 75

solvency, adhesion, cohesion, chemical reactivity, thermal stability

Front 76

what are 4 categories of organic molecules?

Back 76

carbohydrates, lipids, proteins, nucleic acids/nucleotides

Front 77

what element makes elements organic?

Back 77

carbon

Front 78

what makes carbon so versatile?

Back 78

it has 4 valence electrons and bonds with other atoms that provide it with 4 more filling its valence shell; its atoms readily bond with each other and can form long chains, branched molecules and rings (carbon backbones); forms covalent bonds with hydrogen, oxygen and sulfur

Front 79

what is a functional group?

Back 79

small clusters of atoms determining many properties of organic molecules

Front 80

what are the 5 functional groups?

Back 80

hydroxyl (-OH)
methyl (-CH3)
carboxyl (-COOH)
amino (-NH2)
phosphate (-H2PO4)

Front 81

what are monosaccharides?

Back 81

carbohydrates, simple sugars, contain a hydroxyl (-OH) group

Front 82

name 3 monosaccharides and give their molecular formulas

Back 82

glucose, fructose, galactose; all share same molecular formula C6H12O6 (but different structural formula so isomers of each other)

Front 83

disaccharides

Back 83

sugars composed of two monosaccharides

Front 84

name the 3 disaccharides and their sugars

Back 84

sucrose = glucose + fructose
lactose = glucose + galactose
maltose = glucose + glucose
(all share H OH bond in center)

Front 85

polysaccharides

Back 85

long chains of glucose

Front 86

name 3 polysaccharides and their use in the body

Back 86

glycogen= energy storage, made in cells of liver, muscles, brain, uterus, vagina;
starch= energy storage of plants, digestible in human diet;
cellulose= structural, in cell walls of plants, humans ingest as dietary fiber

Front 87

what are the functions of carbohydrates?

Back 87

sources of energy; external surface of cell membrane; dietary fiber

Front 88

polymer

Back 88

large molecules made of a repetitive series (bonds) of identical subunits of monomers (smaller molecules)

Front 89

triglyceride

Back 89

composed of 3 fatty acids covalently bonded to a 3 carbon alcohol called glycerol
(each is formed by dehydration synthesis so water is a by-product)

Front 90

triglycerides are composed of which functional groups?

Back 90

glycerol contains a hydroxyl group (-OH)
each fatty acid contains a carboxyl group (-COOH) on one end and a methyl (-CH3) on the other end

Front 91

saturated fats

Back 91

all carbons are filled up with hydrogen (single covalent bonds)
cannot carry more hydrogen

Front 92

unsaturated fats

Back 92

have a double (=) covalent bond on the carbon so can potentially hold more hydrogen

Front 93

fats

Back 93

generally solid at room temperature
(ex. lard, butter, bacon fat)

Front 94

oils

Back 94

generally liquid at room temperature
(ex. peanut, olive, corn oils)

Front 95

what makes a triglyceride a neutral fat?

Back 95

once they are covalently bonded to glygerol they can no longer donate a proton to a solution and therefore are no longer an acid

Front 96

what are 3 functions of triglycerides?

Back 96

energy storage, insulation, shock absorption (for vital organs in the form of adipose tissue)

Front 97

phospholipid

Back 97

have a phosphate group (instead of one of the fatty acids) which is linked to other functional groups; the two fatty acid "tails" are hydrophobic but the "head" (phosphate) is hydrophilic (so they are amphiphilic)

Front 98

what are the functions of a phospholipid?

Back 98

structural foundation of cell membranes; aid in fat digestion

Front 99

steroid

Back 99

lipid with 17 of its carbon atoms arranged in 4 rings

Front 100

what is the parent steroid?

Back 100

cholesterol, and all other steroids are synthesized from it

Front 101

what are the functions of steroids?

Back 101

important component of cell membranes; required for proper nervous system function

Front 102

amino acids

Back 102

have central carbon atom with an amino functional group (-NH2) and a carboxyl group (-COOH) bound to it

Front 103

how many amino acids?

Back 103

20

Front 104

Rgroup

Back 104

third functional group of amino acids; amino acids only differ in Rgroup; attached to the central carbon; some hydrophilic some hydrophobic (so proteins as a whole often amphiphilic)

Front 105

peptides

Back 105

any protein molecule composed of 2 or more amino acids joined by a peptide bond (formed by dehydration synthesis); joins the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another

Front 106

how are peptides named?

Back 106

by the number of amino acids;
dipeptides = 2 amino acids
tripeptides = 3 amino acids
oligopeptides = 10-15 amino acids
polypeptides = more than 15 amino acids

Front 107

primary protein structure

Back 107

sequence of amino acids; order coded for in genes

Front 108

secondary protein structure

Back 108

coiled or springlike shape (called alpha helix) or folded shape (called beta sheet) held together with hydrogen bonds between slightly negative C=O group of one bond and slightly positive N-H group of another

Front 109

tertiary protein structure

Back 109

further bending or folding of proteins resulting from hydrophobic Rgroups associating with each other and avoiding water and hydrophilic Rgroups attracting to surrounding water

Front 110

what are the functions of proteins?

Back 110

structure, communication, membrane transport, recognition and protection, movement, cell adhesion

Front 111

how does a protein become denatured?

Back 111

extreme heat or pH imbalances usually destroy the function of a protein

Front 112

enzyme

Back 112

proteins functioning as biological catalysts (speeding up reactions)

Front 113

substrate

Back 113

substance an enzyme acts upon (action)

Front 114

active site

Back 114

region of an enzyme (protein) where the 2 substrates bond

Front 115

activation energy

Back 115

energy needed to get the reaction started (enzymes lower amount of energy needed)

Front 116

how does an enzyme work?

Back 116

substrate molecule approaches active site on enzyme (usually has 2 active sites for 2 substrates) and binds to it forming substrate-enzyme complex, enzyme either breaks apart (using hydrolysis) or forms a compound (dehydration synthesis)

Front 117

substrate-enzyme complex

Back 117

site on enzyme that is substrate enzyme specific, like a lock and key

Front 118

co-factor

Back 118

inorganic non-proteins bind to enzymes, stimulates folding into shape activating active site

Front 119

co-enzyme

Back 119

organic co-factors, accept electrons from an enzyme in one metabolic pathway and transfer them to an enzyme in another

Front 120

nucleotides

Back 120

organic compounds with 3 components; a single or double carbon-nitrogen ring (nitrogenous base), a monosaccharide, and 1 or more phosphate groups

Front 121

name 3 nucleotides and their functions

Back 121

ATP= adenosine triphosphate, energy transfer molecule; GTP= guanosine triphosphate, used in energy transfers; cAMP= cyclic adenosine monophosphate, conversion of ATP, "second messenger" activating metabolic effects w/in a cell

Front 122

ATP

Back 122

most important energy transfer molecule, releases energy in seconds, continually replenished

Front 123

DNA: location and function

Back 123

deoxyribonucleic acid; nucleotide; genetic material; located in nucleus (does not leave); double helix; 100 million to 1 billion nucleotides long; deoxirobose is sugar

Front 124

nucleotides

Back 124

have a nitrogenous base, a sugar and a phosphate group
(ex. RNA, DNA)

Front 125

RNA: location and function

Back 125

ribonucleic acid; nucleotide; interprets code of DNA and expresses it; leaves the nucleus; single stranded; 70,000 to 100,000 nucleotides long; ribose is sugar

Front 126

monomers and base pairs of DNA

Back 126

monomers (bases): A (adenine), T (thymine), C (cytosine), G (guanine); A&T paired, form 2 hydrogen bonds; C&G paired, form 3 hydrogen bonds

Front 127

monomers and base pairs of RNA

Back 127

monomers (bases): A (adenine), U (uracil), C (cytosine), G (guanine); A&U paired, C&G paired

Front 128

transcription

Back 128

process of carrying genetic instructions from DNA to RNA, triggered by chemical messengers in cytoplasm entering the nnucleus and binding to chromatin at relevant gene site

Front 129

translation

Back 129

converts the language of nucleotides into the language of amino acids; done by ribosomes