Biology 110 : Chapter 2

Front 1

________ make up all matter

Back 1

atoms

Front 2

all objects in the universe are composed of

Back 2

matter and energy

Front 3

matter

Back 3

is any material that takes up space, such as organisms, rocks, the oceans, and gases in the atmospere

Front 4

energy

Back 4

is the ability to do work(moving matter)

Front 5

heat, light, and chemical bonds are all forms of

Back 5

energy

Front 6

the matter that makes up every object in the universe consists of one or more

Back 6

elements

Front 7

objects are made up of

Back 7

matter

Front 8

matter is made up of

Back 8

elements

Front 9

cannot be broken down into other substances

Back 9

elements

Front 10

element

Back 10

a pure substance that cannot be broken down by chemical means into other substances

Front 11

Russian chmist Dmitry Mendeleyev invented

Back 11

the periodic table

Front 12

periodic table

Back 12

the chart that labels the elements

Front 13

periodic because

Back 13

the chemical properties of the elements repeat in each column of the table

Front 14

atomic number is located

Back 14

on very top above element name

Front 15

atomic mass is located

Back 15

on very bottom below symbol

Front 16

only about _____ elements are essential to life

Back 16

25

Front 17

bulk elements

Back 17

are required in the largest amounts because they make up the vast majority of ever living cell

Front 18

carbon, hydrogen, oxygen, and nitrogen accounting for 96% of the human body. those four elements are...

Back 18

bulk elements

Front 19

minerals

Back 19

essential elements other than C, H, O, and N.

Front 20

Na, Mg, P, K, and Ca are minerals that are

Back 20

bulk elements

Front 21

trace elements

Back 21

elements that are required in tiny amounts

Front 22

elements are made up of

Back 22

atoms

Front 23

atoms are

Back 23

smallest possible part of an element that retains the characteristics of the element

Front 24

atoms are composed of three types of particles

Back 24

1. protons

2. nuetrons

3. electrons

Front 25

protons

Back 25

carry a positive charge

Front 26

nuetrons

Back 26

are uncharged

Front 27

what together form a central nucleus

Back 27

proton and neutrons

Front 28

electrons

Back 28

negatively charged and surround the nucleus

Front 29

electrons are

Back 29

small compared to protons and neutrons

Front 30

most of atoms mass is concentrated in the

Back 30

nucleus

Front 31

the ______ occupies virtually all of a atoms volume

Back 31

electron cloud

Front 32

electron travels around a hydrogen atoms nucleus at about

Back 32

2200 kilometers per second

Front 33

atomic number

Back 33

the number of protons in the nucleus

Front 34

elements are arranged sequentially in the periodic table by

Back 34

atomic number

Front 35

electrically nuetrall

Back 35

when the number of protons equals the number of electrons

-when it has no not charge

Front 36

ion

Back 36

an atom( or group of atoms ) that has gained or lost electrons and therefore has a net negative or positive charge

Front 37

commonly positively charged ions include

Back 37

H* Na* K*

Front 38

negatively charged ions include

Back 38

I- Cl-

Front 39

ions participate in

Back 39

the transmission of messages in the nervous system

Front 40

mass number

Back 40

total number of protons and neutrons in its nucleus

Front 41

neutrons and protons have same

Back 41

mass

Front 42

subtracting the atomic number from the mass number yields the

Back 42

number of neutrons in a n atom

Front 43

all atoms of an element have the same atomic number but not

Back 43

the same number of neutrons

Front 44

isotope

Back 44

any of these different forms of a single element

- 12C (6 neutrons), 13C( seven neutrons)

Front 45

atomic mass (atomic weight)

Back 45

the average mass of all isotopes

Front 46

many of the known isotopes are

Back 46

unstable and radioactive

Front 47

radioactive

Back 47

emit energy as raps or particles when they break down into stable forms

Front 48

every radioactive isotope has a characteristic

Back 48

half life- time it takes for half of the atoms to emit radiation or decay to a different more stable form

Front 49

radioactive isotopes are useful and also dangerous

Back 49

radioactive isotopes are useful and also dangerous

Front 50

what chemical elements do organisms require in large amounts?

Back 50

Carbon, Oxygen, Hydrogen, and Nitrogen

Front 51

where in an atom are protons, neutrons, and electrons located?

Back 51

protons and neutrons are located in the center and make up the nucleus and the electrons surround the nucleus upto a kilometer away

Front 52

what does an elements atomic number indicate?

Back 52

the number of protons in the nucleus

Front 53

what is the relationship between an atoms mass number and an elements atomic mass?

Back 53

mass number is the total number of protons and neutrons in a nucleus and a atomic mass is the average mass number of all isotopes

Front 54

how do all isotopes of the same element differ from one another?

Back 54

they are distinguished by the number of neutrons in the nucleus

Front 55

atomic number

Back 55

the number of protons in an atoms nucleus

Front 56

mass number

Back 56

the number of portons plus the number of neutrons in an atoms nucleus

Front 57

isotope

Back 57

any of the different forms of the same element, distinguished form each other by the number of neutrons in the nucleus

Front 58

atomic mass

Back 58

the average mass of all isotopes of an element

Front 59

atoms are organized into

Back 59

molecules

Front 60

molecule is

Back 60

two or more chemically joined atoms

Front 61

compound

Back 61

a molecule composed of two or more different elements

Front 62

H2O is a

Back 62

compound

Front 63

scientists use molecular formulas to

Back 63

describe the chemical structure of a molecule.

Front 64

molecular formula example

Back 64

CH4= one carbon atom attached to four hydrogen atoms

Front 65

orbitals

Back 65

term to describe the most likely location for an electron relative to its nucleus

Front 66

each orbital can hold up to

Back 66

two electrons

Front 67

energy shell

Back 67

a group of orbitals that share the same level

Front 68

lowest energy shell contains

Back 68

one orbital and two electrons

Front 69

after the first energy shell each shell can contain

Back 69

up to eight electrons in four orbitals

Front 70

valence shell

Back 70

atoms outermost occupied energy shell

Front 71

atoms are most stable when

Back 71

their valence shells are full

Front 72

chemical bond

Back 72

an attractive force that holds atoms together

Front 73

the three types of chemical bonds important in biology

Back 73

covalent bond

ionic bond

hydrogen bond

Front 74

covalent bond

Back 74

two atoms share pairs of electrons

-strong

Front 75

ionic bond

Back 75

one atom donates one or more electrons to another atom, forming oppositely charged ions that attract each other

-strong but breaks easily in water

Front 76

hydrogen bond

Back 76

an atom with a partial negative charge attracts an atom with a partial positive charge. hydrogen bonds form between adjacent molecule or between different parts of a large molecule

-weak

Front 77

in a covalent bond

Back 77

atoms share electrons

Front 78

most bonds in biological molecules are

Back 78

covalent

Front 79

covalent bonds

Back 79

two atoms bonding to fill their valence shell

Front 80

covalent atoms are usually depicted as lines between interacting atoms

Back 80

each line represents one bond

Front 81

each bond contains

Back 81

two elements, one from each atom

Front 82

electronegativity

Back 82

a measure of an atoms ability to attract electrons

Front 83

nonpolar covalent bond

Back 83

where both atoms exert approximtely equal pull on their shared electrons

Front 84

a bond between two atoms of the same element is

Back 84

nonpolar

ex. H2, N2, and O2

Front 85

when two atoms have similar electronegativity and bond they are

Back 85

nonpolar covalent bond

Front 86

polar covalent bond

Back 86

one nucleus exerts a stronger pull on the shared electrons than does the other nucleus

- occurs when a highly electronegative atom pairs with a less electronegative partner

-has positive and negative end

Front 87

has positive and negative end

Back 87

polar covalent bond

Front 88

polar covalen bonds are critical to biology because

Back 88

they are responsiblie for hydrogen bonds which helps define water and the shapes of DNA and proteins

Front 89

in an ionic bond

Back 89

one atom transfers electrons to another atom

Front 90

ionic bond

Back 90

when it makes more sense to release the outer valence electrons to other atoms to fill their valence shell

-in turn both valence shells become full

Front 91

the atom that has lost electrons carries a

Back 91

positive charge

Front 92

the atom that has gained electrons aquires a

Back 92

negative charge

Front 93

ionic bonds tend to form between

Back 93

an atom whose outermost shell is almost empty and on whos valence shell is nearly full

Front 94

two atoms of similar electronegativity share electrons equally in

Back 94

nonpolar covalent bonds

Front 95

if one atom tugs at the shared electrons much more than the other it is a

Back 95

covalent polar bond

Front 96

if one atom is so electronegative that it rips electrons from another atoms valence shell it is a

Back 96

ionic bond

Front 97

bond type depends on the

Back 97

differnece in electronegativity

Front 98

example of emergent properties

Back 98

sodium + chloride = table salt

and

methane= carbon (solid) + hydrogen (gas)

Front 99

electron hogging atom has as

Back 99

partial negative charge

Front 100

less electro negative partner has a

Back 100

electron deficit and partial positive chargw

Front 101

hydrogen bond

Back 101

opposite partial charges on adjacent molecultes, or within a single large molecule attract each other

Front 102

partial charges on polar molecules create

Back 102

hydrogen bonds

Front 103

the atom with the partial positive charge in a hydrogen bond is always

Back 103

hydrogen

Front 104

the atom with the partial negative charge in a hydrogen bond is

Back 104

a highly electronegative atom

Front 105

the partial charges on O and H cause water molecules to

Back 105

stick to one another and to some other substances (example of an emergent property)

Front 106

hydrogen bonds are _______ compared with ionic and covalent obnds

Back 106

relatively weak

Front 107

hydrogen bonds help stailize some

Back 107

large molecules, including proteins and dna

Front 108

bonds break and form in

Back 108

chemical reactions

Front 109

chemical reaction

Back 109

two or more molecules swap their atoms to yield different molecules= some break and new ones form

Front 110

life exists because of thousands of

Back 110

chemical reactions

Front 111

reactants

Back 111

starting materials (molecules before chemical reaction/ before math)

Front 112

products

Back 112

results of the reaction (after math)

Front 113

each side of a chemical equation shows the

Back 113

same number of atoms of each element

- atoms are neither created nor destroyed in reactions , just rearranged

Front 114

how are atoms, molecules, and compounds related?

Back 114

atoms make up molecules and are considered to be the smallest possible part of an element that retains the characteristics of the element, molecules combine and rearrange themselves in the act of a chemical reaction which creates a compound (such as H2O)

Front 115

how does the number of valence electrons determine an atoms tendency to form bonds?

Back 115

if an atoms is close to filling its valence shell and if it is has only one or two electrons in its valence shell it is more likely to form bonds due to ionic and covalent bonds.

Front 116

explain how electronegativity differences between atoms result in nonpolar covalent bonds, polar covlent bonds, and ionic bonds

Back 116

in nonpolar covalent bonds both atoms have near same elctronegtivity (bond between two atoms of the same element is nonpolar)

in polar covalent bonds one atom has a high electronegtivity and the other is less electronegative

in ionic bonds two ions with completely different electronegativity values bond

Front 117

polar covalent bonds are responsible for

Back 117

hydrogen bonds

Front 118

what is the relationship between polar covalent bonds and hydrogen bonds

Back 118

polar covalent bonds are responsible for hydrogen bonds

because there is a atoms with a high electronegativity the hydrogen which is partially positive latches on

Front 119

what happens in a chemical reaction?

Back 119

two or more molecules swap their atoms to yield different molecules

- break and form new bonds

- has reactants and products

- atoms are rearranged

Front 120

hydrogen bonds contribute to a property of water called

Back 120

cohesion

Front 121

cohesion

Back 121

the tendency of water moelcules to stick together

Front 122

surface tension

Back 122

the tendancy of a liquid to hold together at its surface is called surface tension

Front 123

water has a high

Back 123

surface tensions because it is cohesive

Front 124

reasons water is essential to life

Back 124

- it is cohesive

- many substances dissolve in water

- water regulates temperature

- water expands as it freezes

- water participates in lifes chemical reactions

Front 125

water is a

Back 125

solvent= a chemical in which other substances dissolve in

Front 126

the solutes are

Back 126

the dissolved substances

Front 127

solution

Back 127

is one or more solutes dissolved in a liquid solvent

Front 128

scientists divide chemicals into two categories based on solubility in water

Back 128

hydrophilic and hydrophobic

Front 129

hydrophilic substances are

Back 129

are either polar or charged so they readily dissolve in water

Front 130

hydrophobic substances are

Back 130

are nonpolar molecules made mostly of carbon and hydrogen

- do not dissolve in or form hydrogen bonds with water

Front 131

water regulates temperature

Back 131

water regulates temperature

Front 132

evaporation is

Back 132

the conversion of aliquid into a vapor

Front 133

water expanding as it freezes benefits

Back 133

aquatic organisms

Front 134

how is cohesion important to life?

Back 134

cohesion is what keeps water from evaporating instantly and thus not allowing life to persisit

Front 135

differentiate between hydrophilic and hydrophobic molecules

Back 135

hydrophilic molecules are either polar or charged and they dissolve in water; while hydrophobic molecules are nonpolar molecules that do not dissolve in or form hydrogen bonds with water

Front 136

how does water help an organism regulate its body temperature?

Back 136

hydrogen bonds that hold water molecules together tend to counteract the fact that moleules absorb energy as they move faster so water needs more heat to raise its temperature. body regulates temperature so we dont over heat too quickly and dont freeze instantaneously

Front 137

how do the different densities of ice and water affect life?

Back 137

the more dense ice sinks to the bottom of water while the less dense ice floats on the surface of the denser liquid water which allows for aquatic organisms not to be frozen in the water below.

- the less dense ice traps heat in water so organisms do not freeze

Front 138

how does water participate in the chemistry of life?

Back 138

water is either a reactant or a product in almost all of lifes chemical reactions

Front 139

H+ ions are

Back 139

one of the most important substances dissolved in water

Front 140

H+ ionis a

Back 140

hydrogen atoms stripped of its electron (simply a proton)

too much or too little can ruin shapes of critical molecules inside cells making cells nonfunctionals

Front 141

neutral solution

Back 141

has same amount of molecules split up

Front 142

acid

Back 142

is a chemical that adds H+ to a solution

- makes concentration of H+ ions exceed that of the OH- ions

Front 143

base

Back 143

the opposite of an acid

- makes the concentration of OH- ions exceed the concentration of H+ ions

- they come apart to directly add OH- ions to the solution, or they absorb H+ ions

Front 144

acids and bases combined

Back 144

neutralize each other

Front 145

pH scale

Back 145

measure of how acidic or basic a solution is

- ranges from 0-14

- 7 being neutral

- less than 7 being acidic

- alkaline (basic) is pH greater than 7

Front 146

alkaline

Back 146

a basic solution with a pH greater than 7

Front 147

each unit on the pH scale represents a

Back 147

10 fold change in H+ concentration

Front 148

organisms can maintain homeostasis because of

Back 148

buffer systems

Front 149

buffer systems

Back 149

pairs of weak acids and bases releaseing H+ into the solution, restoring acidity; or the buffer consumes the excess H+ in the solution ...keeping the pH of the solution relatively constant.

Front 150

how do acids affect a solutions H+ concentration?

Back 150

acids make the concentration of H+ exceed the concentration of OH-

Front 151

how do the values of 0,7, and 14 relate to the pH scale?

Back 151

0=the most acidic

7=neutral

14= most basic (alkalotic)

Front 152

how do buffer systems regulate the pH of a fluid?

Back 152

buffer systems release H+ into the solution which either restores the acidity or if too much H+ is present the buffer consumes the excess H+

Front 153

organisms are composed mostly of

Back 153

water and organic molecules

Front 154

organic moleucles

Back 154

chemical compounds that contain both carbon and hydrogen

Front 155

autotrophs can

Back 155

produce all he organic molecules they require

Front 156

heterotrophs get organic molecules through

Back 156

food

Front 157

organic molecules consisting almost entirely of carbon and hydrogen are called

Back 157

hydrocarbons

-methane is an example

Front 158

many organic compounds also include

Back 158

oxygen, nitrogen, phosphorus or sulfur

Front 159

the 4 most abundant types of organic molecules in life are

Back 159

1. carbohydrates

2. lipids

3. proteins

4. nucleic acids

Front 160

vitamins are

Back 160

biologically important organic compounds

Front 161

proteins, nucleic acids, and some carbohydrates all share a property in common with another

Back 161

they are chains of small molecular subuintscalled monomer

Front 162

polymers

Back 162

are linked together monomers

Front 163

monomer

Back 163

rail car

Front 164

polymer

Back 164

train

Front 165

dehydration synthesis (condensation reaction)

Back 165

links the monomers together to produce new muscle proteins and other polymers

Front 166

dehydration synthesis

Back 166

a protein called an enzyme removes an OH from one molecule and a hydrogen atom from another, forming H20 and an new covalent bond between the two smaller components

-water is lost

Front 167

hyrolysis

Back 167

breaking covalent bods that link monomers

-enzymes use atoms from water to add a hydrozyl group to one molecule and a hydrogen atom to another

-break down proteins and other polymers in food

Front 168

organic compound

Back 168

contains carbon atoms

Front 169

carbohydrates include

Back 169

simple sugars and polysaccharides

Front 170

carbohydrates

Back 170

organic molecules that consist of carbon, hydrogen, and oxygen

-often in proportion 1:2:1

Front 171

the simplest of the four main types of organic comounds

Back 171

carbs

Front 172

the two main groups of carbs are

Back 172

simple sugars and complex carbohydrates

Front 173

simple sugars

Back 173

monosaccharides

disaccharide

Front 174

monosacchairdes

Back 174

the smallest carb, usually contain five or six carbon atoms

Front 175

disaccharide

Back 175

two monosaccharides joined by dehydration synthesis

-lactose is an example of a disaccharide

Front 176

mono and sdisacchrides are called

Back 176

sugars or simple carbs

Front 177

simple sugars functions in cells is to

Back 177

provide a ready source of energy, which is realeased when their bonds are broken

Front 178

short chains of monosaccharides on cells surfaces are importantin immunity because

Back 178

the combination of carbs attached to the surface of his or her red blood cells tells a persons blood type

Front 179

complex carbs

Back 179

polysaccharides

Front 180

polysaccharides

Back 180

complex carbs, huge molecules consisting of hundreds of monosaccharide monomers

-examples= cellulose, starch, glycogen, and chitin

all long chains of glucose but differ by the orientation of the bonds that link the monomers

Front 181

cellulose forms

Back 181

part of plant cell walls

- carbon fibers, wood, and paper consis largely of cellulose

Front 182

most common organic compound in nature is

Back 182

ellulose

Front 183

humans cannot digest

Back 183

cellulose

Front 184

cellulose is

Back 184

fiber

Front 185

starch and glycogen are

Back 185

polysaccharides with similar structures and functions

-both storage molecules that readily break down into their glcose monomers when cells need a burst of energy

- most plants store starch

-glycogen occurs in animal and fungal cells

Front 186

glycogen occurs in

Back 186

animal and fungal cells

Front 187

most plants store

Back 187

starch

Front 188

chitin

Back 188

resembles a glucose polymer, excpt that it also contains nitrogen atoms

-it is tought, flexible, and biodegradable.

-surgical thread

Front 189

lipids are

Back 189

hydrophobic and energy rich

Front 190

lipids

Back 190

organic compounds with one property in common : they do not dissolve in water

Front 191

lipids are hydrophobi because

Back 191

they contain large areas dominated by nonpolar carbon-carbon and carbon-hydrogen bonds.

Front 192

lipids are not

Back 192

polymers consisting of long chains of monomers

Front 193

two groups of lipids

Back 193

trglycerides and sterols

Front 194

phospholipids

Back 194

lipid

- forms the majority of cell membranes

Front 195

sucralose

Back 195

sweetener closely related to sucrose except that three chlorine atoms replace three of sucroses hydroxyl groups

Front 196

triglyeride

Back 196

consists of three long hydrocarbon chains called fatty acids bonded to glycerol, a three carbon molecule that forms the triglyerides backbone

Front 197

cells use dehydration synthesis to produce

Back 197

triglycerides

Front 198

each fatty aid has a

Back 198

carboxyl group

Front 199

carboxyl group

Back 199

a carbon atom double bonded to one oxygen and single bonded to another oxygen carrying a hydrogen bond

Front 200

enzymes link

Back 200

the fatty acids to glycerol

Front 201

fatty acids

Back 201

three long hydrocarbon chains

Front 202

glycerol

Back 202

three carbon molecule that forms the triglyerides backbone

Front 203

each triglyceride yields

Back 203

three water molecules

Front 204

triglycerides are commonly known as

Back 204

fats

Front 205

fats

Back 205

saturated and unsaturated

Front 206

the degree of saturation is a measure of a fatty acids

Back 206

hydrogen content

Front 207

saturated fatty acid contains

Back 207

all the hydrogens it possibly can

- single bonds connect all the carbons, and each carbon has two hydrogens

Front 208

in unsaturated fats

Back 208

one or more double bonds bend the fatty acid tails to make the lipid more fluid

-vegetable oil

Front 209

unsaturated fatty acid

Back 209

has at least one double bond between carbon atoms

Front 210

polyunsaturated fat has

Back 210

many such double bonds between carbon atoms

Front 211

the double bonds in unsaturated lipids cause

Back 211

kinks to form in the fatty acid tails

Front 212

partial hydrogennation

Back 212

adds hydogen to the oil to solidify it

- paritally saturating a formally unsaturated fat

Front 213

trans fats

Back 213

are unsaturated fats whose fatty tails are straight, not kinked

- byproduct of parital hydrogenation

Front 214

in animals there are

Back 214

white adipose tissue and brown adipose tissue

Front 215

white adipose tissue

Back 215

forms most of the fat in human adults, helping to retain body heat as insulation

Front 216

brown adipose tissue

Back 216

releases heat energy that kees infants and hibernating mammals warm

Front 217

sterols

Back 217

lipids that have four interconnected carbon rings

-vitamin d and cortisone and cholestorl

Front 218

______ is a key part of animal cell membrances

Back 218

cholesterol

Front 219

cholesteroll is a starting material to make other lipids

Back 219

such as sex hormones testosterone an destrogen

Front 220

______ do more jobs in the cell than any other type of biological molecule

Back 220

proteins

Front 221

these molecules control what enters or leaves a cell (through membrane channels), carry oxygen in blood (hemoglobin), aid in blood clotting, build hair and fingernails (keratin), copy genetic material, support the bodys tissues(collagen), participate in immunity(antibodies), break apart food molecuels(digestive enzymes), allow for muscle contraction (actin and myosin)

Back 221

proteins

Front 222

protien

Back 222

a chain of monomers called amino acids

Front 223

amino acids

Back 223

have a central carbon atom bonded to four other atoms or goups of atoms

- one is a hydrogen atom, another is a carboxyl group, a third is a amino group, and the fourth is a side chain or R group

Front 224

amino group

Back 224

nitrogen atomsingle bonded to two hydrogen atoms

Front 225

R group

Back 225

side chain which can be any of 20 chemical groups

Front 226

lifes proteins are composed of

Back 226

20 types of amino acids

Front 227

_______ distinguish the amino acids in a protein from one another, and they have diverse chemical structures

Back 227

r groups

Front 228

r groups are

Back 228

both complex and simple

both acidic and basic

hydrophilic and phydrophobic

Front 229

20 amino acids are like the

Back 229

alphabet

Front 230

peptide bond

Back 230

forms by dehydration synthesis is the covalent bond that links each amino acid to its neighbor

Front 231

two linked amino acids for a

Back 231

dipeptide

Front 232

three linked amino acids form a

Back 232

tripeptide

Front 233

long chains of amino acids are caled

Back 233

polypeptides

Front 234

polypeptide is alled a

Back 234

protein once it folds into its functional shape

-protein may consist of one or more polypeptide chains

Front 235

8 proteins in the body must come from

Back 235

protein rich foods

-digestive enxymes then catalyze the hydrolysis reactions that break peptide bonds and relsase amino acids from proteins in food

- the body then uses these monomer to build its own polypeptides

Front 236

each amino acid structure has

Back 236

a carbon bonded with a

-hydrogen atom

-amino group= NH2

-carboxyl group

-R group= sdie chain which can be any of 20 chemical groups

Front 237

dipeptide formation

Back 237

amino acid + amino acid becomes dipeptide bond through dehydration synthesis (extracts H20)

Front 238

dipeptide breakdwon

Back 238

dipeptide goes through hydrolysis (gains H20) and seperates into two amino acids

Front 239

________ exist as long chains inside cells

Back 239

polysaccharides

Front 240

polypeptide chain folds into

Back 240

a unique three dimensional structure determined by the order and kinds of amino acids

Front 241

four levels of protein structure

Back 241

primary structure

secondary structure

tertiary structure

quaternary structure

Front 242

primary structure in protein structure

Back 242

amino acid sequence of polypeptide

Front 243

the primary structure then

Back 243

folds and curls the amino acid chaines to form secondary structure

Front 244

secondary structure of protein structure

Back 244

localized areas of colis, sheets, and loops withing a polypeptide

Front 245

secondary structures

Back 245

alpha helix

beta sheet (individualy seperate)

Front 246

teriary structure

Back 246

overall shape of one polypeptide

-has both alpha helix and beta sheet

Front 247

quaternary structure

Back 247

overall protein shape, arising from interaction between the multiple polypeptides that make up the functional protein.

Front 248

the four levels of protein structure

Back 248

the amino acid sequence of a polypeptide forms the primary structure, while hydrogen bonds create secondary structures such as a helix or sheet. The tertiary structure is the overall three dimensional shape of a protein. The interaction of multiple polypeptides forms the proteins quaternary structure

Front 249

each protein can have multiple areas fo

Back 249

secondary structure

Front 250

tertiary structure

Back 250

overall shape of a polypeptide, arising primariy through interactions between R groups and water.

- in cells water molecules surround each polypeptide

-hydrophobic r groups move away water toward the proteins interior/ the hydrogen bonds form between the peptide backbone and some R groups (rarely ionic bonds)

Front 251

quarternary structure

Back 251

shape arises from interactions between multiple polypeptide subunits of the same protein

Front 252

______ are vulnerable to external conditions that alter their shapes

Back 252

proteins

Front 253

examples of things that can disrupt the hydrogen bonds that maintain the proteins secondary and tertiary structures

Back 253

heat, excessive salt, or the wrong pH

Front 254

denatured

Back 254

if a proteins structure is modified enough to destroy its function

- if it can no longer do its job

Front 255

preserving foods or heating foods we are

Back 255

denaturing microbial proteins

Front 256

when functional proteins are gone, microbes dies and the foods self life is extended

Back 256

when functional proteins are gone, microbes dies and the foods self life is extended

Front 257

an organisms genetic code specifies the

Back 257

amino acid sequence of each protein

Front 258

a _______ may alter a proteins primary structure

Back 258

genetic mutation

Front 259

geetic mutations often harmful because

Back 259

they result in misfolded, nonfunctional proteins

Front 260

nucleic acids

Back 260

store and transmit genetic information

Front 261

nucleic acid is a

Back 261

polymer consisting of monomers called nucleotides

Front 262

cells contain two types of nucleic acids

Back 262

deoxyribnucleic acid (DNA)

ribonucleic acid (RNA)

Front 263

nucleotide

Back 263

monomer that consists of three compounds

-center is a five carbon sugar, ribose in RNA, and deoxyribose in DNA

-attached to one of the sugar carbon atoms is at lease one phosphate group

- opposite side of sugar is bonded to a nitrogenous base (A, C, G , T)

Front 264

nitrogenous base

Back 264

adenine, guanine, thymine, cytosine, or uracil

Front 265

DNA contains

Back 265

A C G T

Front 266

RNA contains

Back 266

A C G U

Front 267

dehydration synthesis links

Back 267

nucleotides together

Front 268

in a dehydration synthesis

Back 268

a covalent bond forms between the sugar of one nucleotide an the phosphate group of its neighbor

Front 269

DNA polymer is a

Back 269

double helix

- alternating sugars and phosphates for the rails of the staircase

- nitrogenous bases form the fungs

-hydrogen bonds between the bases hold the two strands of nucleotides together (helixs)

A - T , C - G

-helixes are complementary

Front 270

DNA has that RNA doesnt

Back 270

T = thymine

Front 271

RNA has that DNA doesnt

Back 271

U = Uracil

Front 272

nucleic acid forms through

Back 272

dehydration synthesis

Front 273

nucleic acid breaksdown my

Back 273

hydrolysis

Front 274

DNAs main function is to

Back 274

store genetic info

- with thehelp of RNA its sequence of nucleotides tells a cell which amino acids to string together to form each protein

Front 275

many of evolutions changes occur due to

Back 275

slight changes in dna from generation to generation, coupled with natural selection

Front 276

RNA is typically

Back 276

single stranded

-enables cells to use the protein encoding info in DNA

-carries adenosine triphosphate (ATP) whih carries the enrgy that cells use in many biological functions

Front 277

what is the relationship between hydrolysis and dehydration synthesis?

Back 277

hydrolysis is the addition of H20 molecule which breacks down polymers into monomers

and

dehydrations synthesis is the enzyme that removes an OH from one moelcules and a hydrogen atom from another thus removing H2O and joins monomers into polymers

Front 278

describe the monomers that form polysaccharides, proteins, and nucleic acids

Back 278

the monomers that form polysaccharides are monosaccharides( usually contain 5 or 6 carbon atoms)

the monomers that form proteins are amino acids(Carbon bonded with four other atoms or groups of atoms: hydrogen, carboxyl group, amino group, R group)

the monomers that form nucleic acid are nucleotides (DNA and RNA)

Front 279

the monomers that form nucleic acids are

Back 279

the monomers that form nucleic acid are nucleotides (DNA and RNA)

Front 280

the monomers that form carbohydrates are

Back 280

the monomers that form polysaccharides are monosaccharides( usually contain 5 or 6 carbon atoms)

Front 281

examples of carbohydrates and name the function of each

Back 281

simple sugars= monosaccharides and disaccharides= provide quick energy

complex carbohydrates (glucose, starch, glycogen, chitin)= polymers of monosaccharides= support cells and organisms( cellulose and chitin) / store energy (starch, glycogen)

Front 282

simple sugars=

Back 282

monosaccharides and disaccharides= provide quick energy

Front 283

complex carbohydrates

Back 283

(glucose, starch, glycogen, chitin)

-polymers of monosaccharides

-support cells and organisms( cellulose and chitin)

-store energy (starch, glycogen)

Front 284

examples of lipids and name the function of each

Back 284

triglycerides (fats)= glycerol + 3 fatty acids= store energy

phospholipids= glycerol+2 fatty acids +phosphate group= form major part of biological membranes

sterols= 4 fused rings, mostly C and H= stabalize animal membrances; sex hormones

Front 285

triglycerides

Back 285

fats

-glycerol + 3 fatty acids

-store energy

Front 286

lipids that are made up of glycerol + 3 fatty acids is

Back 286

triglycerides

Front 287

lipid that stores energy

Back 287

triglycerides

Front 288

phospholipids

Back 288

glycerol+2 fatty acids +phosphate group

-form major part of biological membranes

Front 289

lipids that are made up of glycerol + 2 fatty acids + phosphate is...

Back 289

phospholipids

Front 290

lipid that forms a major part of biological membranes

Back 290

phospholipids

Front 291

sterols

Back 291

4 fused rings, mostly C and H

-stabalize animal membrances; sex hormones

Front 292

lipids that are made up of 4 fused rings made up mostly of C and H

Back 292

sterols

Front 293

lipids that stabalize animal membrances

Back 293

sterols

Front 294

examples of proteins and name the function of each

Back 294

made up of polymers of amino acids

- carry out nearly all the work of the cell

Front 295

examples of nucleic acids and name the function of each

Back 295

DNA & RNA

- made up of polymers of nucleotides

-store and use genetic info and transmit it to the next generation

Front 296

what are the components of a triglyceride

Back 296

made up of fatty acids bonded to glycerol(three carbon molecule that forms the backbone of triglyceride)

each fatty acid has a carboxyl group

- carbon atom double bonded to one oxygen and single bonded to another oxygen carrying a hydroen atom

- 3 H20 molecules per triglyceride

Front 297

what is the significance of a proteins shape and how can that shape be destroyed?

Back 297

the significance of a proteins shape is that the function of a protein is a result of its shape ( contractile, structural, transport, storage, enzymes)

- shape can be destroyed by genetic mutations and denaturization. both alter the primary structure or in denatured the hydrogen bonds are disrupted in secondary or tertiary structure which then destroy the functionality of the protein

Front 298

what are some differences between rna and dna

Back 298

RNA has U , is single stranded , one function is to enable cells to use the protein encoding info in DNA , has ATP which carries the energy that cells use in many biological functions

DNA has T , main function is to store genetic info

Front 299

cells require

Back 299

carbs, lipids, proteins, anc nucliec acids

Front 300

on earth 98.89% of C atoms are

Back 300

C12 with 6 protons and 6 neutrons

Front 301

scientists use the small difference in how many proteins and neutrons C or N has to

Back 301

distinguish between terrestraial and extraterrestrial materials

Front 302

what question were these researchers trying to answer

Back 302

whether the murchison meteor and meteors in the past was how life obtained organic molecules initially

Front 303

why are N15 and C13 called heavy isotopes? how are they different from N14 and C12?

Back 303

they are slightly more abundent in materials from outer space than they are on earth. They contain an extra neutron

Front 304

both groups of researchers collected samples from the meteorites interior. why does the sample location matter?

Back 304

because the sample on the outside could have been contaminated

Front 305

how would the results have differed if the amino acids and bases were contaimants acquired after the meteorite fell to earth?

Back 305

the results would have shown less C13 and N15 parts per thousand and more C12 and N14

Front 306

all matter can be broken down into pure substances called

Back 306

elements

Front 307

elements are

Back 307

fundamental types of matter

Front 308

bulk elements are

Back 308

essential to life in large quantities

Front 309

trace elements

Back 309

are required in smaller amounts

Front 310

minerals are

Back 310

essential elements other than C,H,O, and N

Front 311

atoms are

Back 311

particles of elements

Front 312

an atom is

Back 312

the smallest unit of an element

Front 313

positively charged protons and neutral neutrons

Back 313

form the nucleus

Front 314

negatively charged, much smaller electrons

Back 314

surround the nucleus

Front 315

elements are organized in the

Back 315

periodic table according to atomic number (the number of protons)

Front 316

an ion is

Back 316

an atom that has gained or lost electrons

Front 317

isotopes of an element differ by

Back 317

the number of neutrons

Front 318

a radioactive isotope is

Back 318

unstable

Front 319

an elements atomic mass reflects

Back 319

the average mass number of all isotopes, wighted by the proportions in which they naturally occur

Front 320

molecule is

Back 320

two or more atoms joined together

Front 321

compound is

Back 321

two or more atoms joined together of different elements

Front 322

electrons determine

Back 322

bonding

Front 323

electrons move

Back 323

constantly in volumes of space called orbitals

- grouped into energy shells

Front 324

an atoms tendency to fill its valence sell with eletrons drives it to form

Back 324

chemical bonds with other atoms

Front 325

in a covalent bond

Back 325

atoms share electrons

Front 326

covalent bonds

Back 326

form between atoms that can fill their valence shells by sharing one or more pairs of electrons

Front 327

atoms in a nonpolar covalent bond share

Back 327

electrons equally

Front 328

highly electronegative atoms in covalent bonds attract

Back 328

electrons away from less electronegative atoms, forming polar covalent bonds

Front 329

nonpolar covalent bonds

Back 329

same electronegativity

share equally

Front 330

polar covalent bonds

Back 330

different electronegativity

dont share equally

Front 331

in an ionic bond

Back 331

one atom transfers electrons to another atom

Front 332

ionic bond is

Back 332

an attraction between two oppositely charged ions

- form when on atom strips one or more electrons from another atom

Front 333

partial charges on polar molecules create

Back 333

hydrogen bonds

Front 334

hydrogen bonds result from the

Back 334

attraction between opposite partial charges on adjacent molecules or within a large molecule

Front 335

bonds break and form in

Back 335

chemical reactions

Front 336

water is significant because

Back 336

cohesive

a solvent

a regulator of temperature

expands as it freezes which makes ice less dense than liquid water

most biochemical reactions occur in watery solutions

Front 337

water molecules stick together

Back 337

cohesive

Front 338

solution consists of a

Back 338

solute dissolved in a solvent

Front 339

water dissolves

Back 339

hydrophillic ( polar and charged) substances but not hydrophobic ( nonpolar) substances

Front 340

water regulates temperature in oganisms because it

Back 340

resists both temp cahnge and evaporation

Front 341

an acids adds a ___ to H20

Back 341

H+

Front 342

base adds a _____ to H20

or removes ____

Back 342

OH-, H+

Front 343

pH scale measures

Back 343

H+ concentration

-neutral 7

-acidic 7>

-basic (alkaline) 7-14

Front 344

buffers consist of

Back 344

weak acid base pairs that maintain the optimal H ranges of body fluids

Front 345

organic molecules consists of small subunits called

Back 345

monomers which link together to form polymers

Front 346

dehydration synthesis is the

Back 346

chemical reaction that joins monomers together, releasing a water molecule

Front 347

hydrolysis reaction

Back 347

uses water to break polymers into monomers

Front 348

carbohydrates include

Back 348

simple sugars and polysaccharides

Front 349

carbs consists of

Back 349

carbs, hydrogen, and oxygen

1:2:1

Front 350

monosaccharides

Back 350

single molecule sugars such asglucose

- two bonded monosaccharides form a disaccharide

Front 351

mono and dissacharides are

Back 351

simple sugars that provide quick energy

Front 352

polysaccharides

Back 352

complex carbohydrates consisting of hundreds of monosaccharides

-provide support and store energy

Front 353

lipids are

Back 353

hydrophobic and energy rich

Front 354

lipids are

Back 354

diverse hydrophobic compounds consisting mainly of C and H

Front 355

triglycerides (fats) consist of

Back 355

glycerol and 3 fatty acids

- store energy, slow digestion, cushion organs, an dpreserve body heat

Front 356

fatty acids may be

Back 356

saturated( no double bonds) or unsaturated ( at least one double bond)

Front 357

sterols

Back 357

-cholestorl and sex hormones

-lipids consisting of 4 carbon rings

Front 358

proteins are

Back 358

complex and highly versatile

Front 359

proteins consists of

Back 359

amino acids which form into polypeptides by forming peptide bonds through dehydration synthesis

Front 360

amino acids form into polypeptides by

Back 360

forming peptide bonds through dehydration synthesis

Front 361

a proteins 3 dimensional shape is vital to its function

Back 361

a denature protein has a ruined shape

Front 362

nucleic acids store and transmit

Back 362

genetic info

Front 363

nucleic acids include

Back 363

dna and rna and are polmers consisting of nucleotides

Front 364

dna carries genetic info and transmits it from generation to generation while

Back 364

rna copies the info, enabling the cell to make protins

Front 365

the atomic mass of an element reflects the total number of

Back 365

protons and neutrons

Front 366

protons and neutrons make up the

Back 366

atomic mass

Front 367

the atomic numbe of the element neon is 10. how many electronsdoes a neutral atom of neon contain?

Back 367

b

Front 368

atomic number is

Back 368

electrons

Front 369

a covalent bond forms when

Back 369

a pair of valence electrons is shared between two atoms

Front 370

the atomic number of silicon is 14. use the concept of energy shells to predict the number of covalent bonds that Si could form

Back 370

4

because first shell takes 2 electrons and the rest of the shells can take up to 8 electrons

Front 371

an ionic bond forms when

Back 371

an electrical atraction occurs between two atoms of different charge

Front 372

a hydrophilic substance is one that can

Back 372

dissolve in water

Front 373

what type of chemical bond is being broken when methane burns in oxygen

Back 373

nonpolar covalent

Front 374

what type of chemical bond forms during a dehydration synthesisreaction

Back 374

covalent

Front 375

a sugar is an example of a ______, whereas dna is a ________

Back 375

carbohydrate, nucleic acid

Front 376

the shape of a protein is determined by

Back 376

- the sequence of amino acids

-chemical bonds between amino acids

-temperatue and pH

Front 377

matter

Back 377

has mass and occupies space

1. liquid

2. gas

3. solid

Front 378

atoms make up all

Back 378

matter

Front 379

atomic number is

Back 379

on top and is the number of number of electrons

Front 380

atomic mass is

Back 380

protons + neutrons

Front 381

protons give an atom

Back 381

identity

Front 382

electrons give an atoms

Back 382

personality

-determines how an atom behaves when it encounters other atoms

Front 383

proton has a charge of

Back 383

+1

amu =1

Front 384

electron has a charge of

Back 384

-1

amu=0

Front 385

ionic bonds form

Back 385

compounds

Front 386

nacl is a

Back 386

ionic bond

Front 387

ionic bonds

Back 387

one element donates an electron which changes the isotope of both charges, making these oppositely charged ions then attract each other

Front 388

ionic bonds

Back 388

give donation and attach

Front 389

covalent bonds form

Back 389

molecules and are strong

Front 390

in covalent bonds atoms

Back 390

share electrons

-ususally allowing both atoms to fill their valence shells

Front 391

hydrogen bonds form between

Back 391

charged molecules

Front 392

hydrogen bonds are

Back 392

individually weak but collectively strong

Front 393

each water molecule can bond to a max of

Back 393

4 other water molecules

Front 394

individual water molecules are

Back 394

covalent bonds

Front 395

collective water molecules are

Back 395

hydrogen bonds

Front 396

water is

Back 396

cohesive and adhesive

Front 397

life began

Back 397

in water and evolved in water for 3 billion years before moving on land

Front 398

our cells are 70-95% water and water is 70% of our body weight

Back 398

our cells are 70-95% water and water is 70% of our body weight

Front 399

these bonds tend to be soluble in water

Back 399

ionic bonds

Front 400

strongest bond

Back 400

covalent bond

Front 401

OH-

Back 401

hydroxide ion

Front 402

bases have more

Back 402

OH- than H+

Front 403

acids have more

Back 403

H+ than OH-

Front 404

organic molecules

Back 404

carbon based

-carbs

-lipids

-proteins

-nucleic acids

Front 405

organic molecule contains

Back 405

hydrogen and carbon

- methane (CH4)

Front 406

simple sugars like glucose and fructose are the

Back 406

main fuel for cellular work

- both soluble in water

Front 407

carb polymers

Back 407

disaccharides and polysaccharides

Front 408

lipid monomers shapes

Back 408

straight is saturated

bent is unsaturated

shorter is glycerol

Front 409

saturated fats can change shape via hydrogenation which creates

Back 409

transfats

Front 410

synthetic anabolic steroids are

Back 410

variants of testosterone

build muscle quickly

Front 411

amino acids are like building blocks

Back 411

20 different types

Front 412

protein polymers

Back 412

polypeptides

Front 413

polypeptides get folded to become

Back 413

proteins

Front 414

all proteins have

Back 414

primary, secondary, and tertiary structures while only some have quaternary structure

Front 415

enzymes

Back 415

proteins that assist in chemical reactions

Front 416

proteins are

Back 416

polypeptides that are folded, twisted, and coiled into unique shapes

- ITS ALL ABOUT THE SHAPE

Front 417

nucleic acid monomers

Back 417

5 types

A C G T U

Front 418

3 parts of a nucleotide

Back 418

- nitrogen containing base

- sugar

- phosphate

Front 419

DNA

Back 419

- sugar is deoxyribose

- bases include A T C G

- double stranded

Front 420

RNA

Back 420

- sugar is ribose

- bases are A U C G

- single stranded

Front 421

dna is transcribed into

Back 421

rna

Front 422

rna is transcribed into

Back 422

proteins

Front 423

nucleic acids do/ do not dissolve in water

Back 423

do

Front 424

water has

Back 424

oxygen atom that is slightly negative

two hydrogen atoms that are slightly positive

Front 425

products of hydrolysis reactions on a triglyceride

Back 425

glycerol and fatty acid

Front 426

during dehydration synthesis

Back 426

an enzyme joins two monomers

water is a byproduct

Front 427

potential causes of proteins not functioning

Back 427

-change in temp near the protein

-decrease in pH

-increase in pH

-increase in nacl concentration

-change in the amino acid sequence

-decrease in nacl concentration

-surrounding solutions shift from water to oil

Front 428

stored in adipose tissue

Back 428

lipids

Front 429

localized three dimensional structure

Back 429

secondary structure

Front 430

overall shape of a chain of amino acids

Back 430

tertiary structure

Front 431

results when R groups move toward or away from water

Back 431

tertiary structure

Front 432

interactions between multiple chains of amino acids

Back 432

quarentary structure

Front 433

what might cause a protein to become non functional

Back 433

-change in temp near the protein

-decrease in pH

-increase in pH

-increase in nacl concentration

-change in the amino acid sequence

-decrease in nacl concentration

-surrounding solutions shift from water to oil

Front 434

name the carbohydrate monomer

Back 434

monosaccharide

Front 435

this monomer attaches to a glycerol backbone

Back 435

fatty acid

Front 436

name the protein monomer

Back 436

amino acid

Front 437

name the nucleic acid monomer

Back 437

nucelotide

Front 438

honey is a mix of these two monosaccharides

Back 438

glucose and fructose

Front 439

name two beneficial lipids found in the human body

Back 439

hormones and cholesterol

Front 440

the number of amino acid types

Back 440

20

Front 441

DNA stores the information to produce

Back 441

proteins

Front 442

this carbohydrate polysaccharide is indigestible to humans

Back 442

cellulose

Front 443

this process changes cis into trans fatty acids

Back 443

hydrogenation

Front 444

this protein assists in chemical reactions

Back 444

enzymes

Front 445

the three parts of a nucleotide are

Back 445

nitrogenous base, phosphate, sugar

Front 446

the average american consumes this many pounds of sugar a year

Back 446

140 lbs

Front 447

a fatty acid with a double bond and less hydrogen is called

Back 447

unsaturated fat

Front 448

four levels of organization of a protein

Back 448

primary

secondary

tertiary

quarenary

Front 449

cytosine is an example of a nucleotide, the four others are

Back 449

uracil or thymine, Cytosine, Adenine