Biochem Quiz 2/test 2

Front 1

__ structure is when the primary and secondary configurations bend and fold into a specific 3d shape.

Back 1

Tertiary Structure; tertiary structure is when the primary and secondary configurations bend and fold into a specific 3d shape

Front 2

tertiary structure results from the interactions between the R groups of the different ______

Back 2

amino acid residues, tertiary structure results from the interactions between the R groups of different amino acid residues

Front 3

__ are covalent bonds that contriube to the stability of the 3d shape of the protein

Back 3

disulfide bridges; disulfide bridges are covalent bonds that contribute to the stability of the 3d shape of a protein

Front 4

R group interations in tertiary structures include __ , ___,___, and ____

Back 4

disulfide bridges, ionic interactions, hydrophobic interactions, and hydrogen bonds

Front 5

In tertiary structure, carboxyl groups interacting with amino groups is an example of __ interactions

Back 5

ionic; in tertiary structures, when carboxy groups interact with amino groups, that is an example of an ionic interaction

Front 6

__ structure refers to the structure of proteins containing more than one polypeptide chain (subunit)

Back 6

quaternary structure; quaternary structure refers to the structure of proteins containg more than one polypeptide chain

Front 7

___ proteins contain only amino acid residues

Back 7

simple; simple proteins only contain amino acid residues

Front 8

Conjugated proteins also contain other components called __ groups

Back 8

prosthetic groups; Conjugated proteins contain prosthetic groups

Front 9

Hemoglobin (hb) is an example of a __ protein with a quaternary structure

Back 9

conjugated protein; hemoglobin is an example of a conjugated protein with a quaternary structure

Front 10

Protein folding occurs during synthesis in the __

Back 10

ER; protein folding occurs during synthesis in the ER

Front 11

Interactions between the ____ --both attraction and repulsion play a role in the folding process

Back 11

side chains; interactions between the side chains--both attraction and repulsion play a role in the folding process

Front 12

Chaperones called ____ proteins assist in the protein folding

Back 12

heat shock proteins; chaperones called heat shock proteins assist in the protein folding

Front 13

__ is the 1 degree component of plaque in Alzheimer's disease

Back 13

amyloid plaque; amyloid plaque is the 1 degree component of plaque in alzheimer's disease

Front 14

__ of a protein results in the loss of its characteristic native structure and function

Back 14

denaturation; denaturation of a protein results in theloss of its characteristic native structure and function

Front 15

Extreme temperatures denature proteins, so most proteins are biologically active b/w __ and __ degree celcius

Back 15

Extreme temperatures denature proteins, so most proteins are biologically active b/w 0-40 degrees celcius

Front 16

Strong acids/bases can denature proteins by affecting the ____

Back 16

salt bridges; strong acids/bases can denature proteins by affecting the salt bridges

Front 17

organic solvents and ___ can cause protein denaturation by disrupting hydrophobic reactions

Back 17

detergents; organic solvents and detergents can cause protein denatuation by disrupting hydrophobic reactions

Front 18

reducing agents such as __ and b-mercaptoethanol, disrupt disulfide bridges and cause protein denaturation

Back 18

urea; reducing agents such as urea and b mercaptoethanol, disrupt disulfide bridges and cause denaturation

Front 19

__ concentration can cause denaturation b/c it binds amino acids ionizable groups followed by h20 solvation and precipitation

Back 19

salt concentration; salt concentration can cause protein denaturation

Front 20

___ ions disrupt salt bridges, bind sulfydryl groups, and cause denaturation

Back 20

heavy metal ions; heavy metal ions can disrupt salt bridges, bind sulfydryl groups, and cause denaturation

Front 21

__ disrupts hydrogen and salt bridges

Back 21

mechanical stress; mechanical stress disrupts hydrogen and salt bridges and can cause denaturation

Front 22

8 things that cause protein denaturation

Back 22

strong acids/bases; extreme temperatures; organic solvents; detergents; reducing agents; salt concentration; heavy metal ions; and mechanical stress

Front 23

Protein denaturation is a precursor for _____

Back 23

protein digestion; protein denaturation is a precursor for protein digestion

Front 24

In ____, the 3d structure is broken and the protein loses its native structure. (uncoiling of protein)

Back 24

protein denaturation; in protein denaturization, the 3d structure is broken and the protein uncoils

Front 25

The amount of __ released when an acid is dissoved in water determines the strength of the acid

Back 25

H+; the amount of hydrogen released when an acid is dissoved in water determines the strength of the acid

Front 26

The more free H+ ions, the __ the acid

Back 26

stronger the acid; the more free hydrogen ions, the stronger the acid

Front 27

hydrogen concentration is expressed as the ___

Back 27

molarity; hydrogen concentration is expressed as the molarity

Front 28

M=moles/L

Back 28

Molarity; Molarity equals moles per liter

Front 29

___ denotes the number of moles of a given substance per liter of solutions

Back 29

Molarity; Molarity denotes the number of moles of a given substance per liter of solution

Front 30

The ____ ion is the most important ion in biological systems due to its effects on protein structure and biological reactions

Back 30

H+; hydrogen ions are the most important ions in biological systems due to its effects on protein structure and biological reactions

Front 31

Acids are proton ___

Back 31

donors; acids are proton donors

Front 32

Protons, hydrogen ion, and H+ are all the same; interchangeable terms; ie proton donor= hydrogen ion donor= H+ donor

Back 32

TRUE

Front 33

Bases are proton ___

Back 33

acceptors; bases are proton acceptors

Front 34

Bases accept protons=accept H+= accept hydrogen ions

Back 34

TRUE

Front 35

bases want to become more positive and therefore accept H+

Back 35

TRUE

Front 36

acids want to be more negative therefore they want to get rid of their positive H+ charges

Back 36

TRUE

Front 37

Stomach acid and battery acid are ___

Back 37

strong acids; stomach acid and battery acid are strong acids with a ph of 0-2

Front 38

lemon juice and vinegar are ___

Back 38

weak acids; lemon juice and vinegar are weak acids with a ph of 3-6

Front 39

pure water is __ with a ph of 7

Back 39

neutral; pure water is neutral with a ph of 7

Front 40

bicarbonate solution is a __

Back 40

weak base; bicarbonate solution is a weak base with a ph of 8-11

Front 41

NaOH, and oven cleaner (KOH) are ___

Back 41

strong bases; NaOH and KOH are strong bases with a ph b/w 12-14

Front 42

__ acids and bases completely dissociate

Back 42

strong; strong acids and bases completely dissociate

Front 43

Organic acids are __ acids and thus only partially dissociate

Back 43

weak acids; organic acids are weak acids and thus only partially dissociate

Front 44

The acid dissociation constant

Back 44

Ka

Front 45

__ represents the strength of an acid

Back 45

Ka

Front 46

The greater the Ka, the __ the acid

Back 46

stronger; the greater the Ka, the stronger the acid

Front 47

Ka=[H+] [A-]/[HA]

Back 47

TRUE

Front 48

Acids are defined by __ concentration

Back 48

H+

Front 49

H+ is not found free in solution and instead combines with a water molecule to form __

Back 49

H30; H+ is not found free in solution and instead combines with a water molecule to form H30

Front 50

H3O+ is a ___ion

Back 50

hydronium ion; H3O+ is an hydronium ion

Front 51

The ph of 7 is considered neutral at 25 degrees celsius b/c at theis ph the concentration of h3o equals the concentrations of OH- in pure water

Back 51

TRUE

Front 52

kw=[h+] [oh-]=1*10^-14

Back 52

water constant

Front 53

pH= -log [H+]

Back 53

TRUE

Front 54

pKa=-log Ka

Back 54

TRUE

Front 55

the smaller the pKa value, the __the acid

Back 55

stronger; the smaller the pKa, the stronger the acid

Front 56

Used in predicting properties of buffer solutions sued to control pH of reaction mixtures

Back 56

henderson-hasselbalch equation

Front 57

pH=pKa+log [A-}/[HA]

Back 57

henderson hasselbalch equation

Front 58

A --solution is one which resists changes in ph when small quantities of an acid or base are added to it

Back 58

buffer solution

Front 59

an acidic buffer has a ph of less than ___

Back 59

7; an acidic buffer has a ph of les than 7

Front 60

a __ buffer has a ph of more than 7

Back 60

basic; a basic buffer has a ph of more than 7

Front 61

Ways the body regualtes ph

Back 61

1. Buffers 2. Co2 eliminated by the lungs 3. Acids and bases eliminated via kidneys

Front 62

blood ph must be kept close to __

Back 62

7.4

Front 63

blood ph above 7.4=___

Back 63

alkalosis

Front 64

blood ph below 7.4=___

Back 64

acidosis

Front 65

body must get rid of __ moles of acid/day (mostly C02)

Back 65

-15

Front 66

ph changes charges on molecules, especially---

Back 66

proteins

Front 67

__ is when measured amounts of base are added to a measured amount of acid

Back 67

titration

Front 68

where ph=pka is called the xxx

Back 68

inflection point; the inflection point is the point where ph=pka of acid

Front 69

at the xxx ph changes very slowly as more base is added

Back 69

inflection point; at the inflection point ph changes very slowly as more base is added

Front 70

buffering region is -- ph unit above and below the inflection point

Back 70

1; the buffering region is 1 ph above and below the inflection point

Front 71

__ is an intracellular physiological buffer

Back 71

phosporic acid; phosphoric acid is an intracellular physiological buffer with a ph of 7.2

Front 72

__ is an extracellular blood buffering system

Back 72

carbonic acid; carbonic acid is an extracellular, blood buffering system

Front 73

dissolved co2 forms __ which reacts to produce bicarbonate ion (HCO3-)

Back 73

carbonic acid; dissoved co2 forms carbonic acid which produces hco3

Front 74

there is a direct relationship b/w blood ph and lung ____.

Back 74

co2 pressure; there is a direct relationship b/w blood ph and lung co2 pressure

Front 75

__ results in co2 trapped in lung tissue

Back 75

pulmonary obstruction; pulmonary obstruction results in co2 trapped in lung tissue

Front 76

A __ lower's blood hco3- concentration and thusly lowers blood ph

Back 76

pulmonary obstruction; pulmonary obstruction lowers blood hco3- concentration and thusly lowers blood ph which causes acidosis and eventually death

Front 77

__ in a solution contain weakly acidic carboxyl and weakly basic amino groups

Back 77

amino acids; amino acids in a solution contain weakly acidic carboxyl groups and weakly basic amino groups

Front 78

Buffers obey ___'s principle

Back 78

le chatleier's principle

Front 79

if a stress is applied to a reaction at equilibrium, the equilibrium will be displaced in the direction that relieves the stress

Back 79

le chatelier's principle

Front 80

At low (acidic) ph, both groups __

Back 80

protenated; at a low ph, both groups are protonated

Front 81

As ph increases, carboxyl group (COOH) DISSOCIATES h+ TO FORM ____ (COO-)

Back 81

carboxylate; as ph increases, carboxyl group dissociates h+ and forms COO-

Front 82

increasing ph results in converstion of H3N+ to __

Back 82

H2N; increasing ph results in conversion of H3N+ to H2N

Front 83

At isoelectric point (p1), amino acid is predominantly ___ form

Back 83

dipolar; at isoelectric point (p1), amino acid is predominantly dipolar form

Front 84

the 2 buffering regions

Back 84

pk1 and pk2

Front 85

pk1=

Back 85

1=2

Front 86

pk2=

Back 86

2=3

Front 87

protein is a __ molecule

Back 87

polar; protein is a polar molecule

Front 88

__ are catalysts that speed up reactions

Back 88

enzymes

Front 89

__ are not involved in the reaction, reduce the activation energy, are highly specific, and can be regulated

Back 89

enzymes

Front 90

enzymes are __

Back 90

proteins

Front 91

__ is what the enzyme is working on

Back 91

substrate; a substrate is what the enzyme is working on

Front 92

Enzyme contains special pocket where amino acid side chains create a 3d surface complementary to that of the substrates

Back 92

active site

Front 93

the number of molecules of substrate converted to product per enzyme molecule per second

Back 93

Turnover number; the turnover number is generally 100-1000/second

Front 94

___ and __ are nonprotein compounds that are needed for enzyme activity

Back 94

coenzymes and cofactors; are nonprotein compounds that are needed for enzyme activitiy

Front 95

Energy utilized by the body is obtained from the energy found in __

Back 95

macronutrients

Front 96

the SI energy unit is the

Back 96

joule

Front 97

__ is the energy needed to increase the temp of 1 gram of water by 1 degree celsius

Back 97

calorie or kilocalorie

Front 98

1 calorie=__ joules

Back 98

4.18; 1 calorie = 4.18 joules

Front 99

__ is the energy needed to incresae the temp of 1kg of water by 1 degree celsius

Back 99

1 kcal or 1000 small calr

Front 100

released energy is referred to as ____

Back 100

free energy; released energy is referred to as free energy

Front 101

Energy available to do work is known as ___ energy

Back 101

free energy;

Front 102

__ energy approaches zero as reaction proceeds to equilibrium.

Back 102

free energy;

Front 103

__ is the change in free energy of the reaction

Back 103

delta G

Front 104

Chem reactions have an energy barrier separating reactants from products callerd ___

Back 104

activation energy

Front 105

Free energy of products-Free energy of reactants=__

Back 105

delta G of a reaction

Front 106

if delta G negative then

Back 106

exothermic

Front 107

__ is energy releasing; net loss of energy and reaction goes as written from A-->B

Back 107

exothermic

Front 108

__ is energy requiring, net gain of energy and reaction does not go spontaneously from a-->b

Back 108

endothermic

Front 109

If delta G positive then

Back 109

endothermic

Front 110

if delta G is 0 then

Back 110

reactants are in equilibrium

Front 111

Intermediate formed during conversion of reactant to product

Back 111

transition state;

Front 112

Catalysts alter the ___

Back 112

activation energy

Front 113

____ binds substrate in a geometry resembling the activated transition state of the molecule

Back 113

transition state stabilization; transition state stabilization binds substrate in a geometry resembling the activated transition state of the molecule

Front 114

Amino acid side groupos participate in acid-base catalysis in which amino acids provide or accept protons

Back 114

TRUE

Front 115

Enzyme binds the substrate in position resembling the _____ of the molecule

Back 115

activated transition state; enzyme binds the substrate in position resembling the activated transition state of the molecule

Front 116

phosphate buffer___ the cell

Back 116

inside the cell

Front 117

Bicarb buffer___ the cell

Back 117

outside the cell

Front 118

___ converts co2 and h2o into h2co3

Back 118

carbonic anhydrase

Front 119

__ is the enzyme found in red blood cells

Back 119

carbonic anhydrase

Front 120

phosphate buffer___ the cell

Back 120

inside the cell

Front 121

Bicarb buffer___ the cell

Back 121

outside the cell

Front 122

___ converts co2 and h2o into h2co3

Back 122

carbonic anhydrase

Front 123

__ is the enzyme found in red blood cells

Back 123

carbonic anhydrase

Front 124

__ is the enzyme that controls the ph of blood

Back 124

carbonic anhydrase

Front 125

lungs eliminate ---

Back 125

co2

Front 126

liver excretes

Back 126

acid

Front 127

__ is the point at which you have equal concentrations of acid and conjugate base

Back 127

pka; pka is the point at which you havve equual concentration of acid and conjugate base

Front 128

pk1 refers to

Back 128

COO-

Front 129

pk2 refers to

Back 129

NH3+

Front 130

pk3 refers to

Back 130

side chain

Front 131

__ is only used when there is a side chain

Back 131

pk3

Front 132

alanine has no side chain and only has pk1 and pk2

Back 132

TRUE

Front 133

the average of pk1 and pk2 is the __

Back 133

isoelectric ph

Front 134

histidine has __pkas

Back 134

3

Front 135

minerals such as fe, zn, mn, fl, ni are __

Back 135

cofactors

Front 136

organic compoungs such as NAD, and FAD are __

Back 136

coenzymes

Front 137

__ are protein and non protein compunds

Back 137

haloenzyme

Front 138

alcohol dehydrenase and pyruvate dehydrogenase are examples of

Back 138

haloenzyme

Front 139

alcohol dehydrogenase needs _ as a cofactor

Back 139

zinc; alcohol dehydrogenase needs zinc as a cofactor

Front 140

pyruvate dehydrogenase needs __ as a coenzyme

Back 140

NAD; pyruvate dehydrogenase needs NAD as a coenzyme

Front 141

zinc is a --

Back 141

cofactors

Front 142

the protein portion of a haloenzyme is called__

Back 142

apoprotein

Front 143

apoprotein + coenzyme/cofactor=

Back 143

haloenzyme

Front 144

tightyly bound conezymes such as FAD have a ___group

Back 144

prosthetic group

Front 145

1 calorie=4.18 joules

Back 145

TRUE

Front 146

1kcal=4.184 kj

Back 146

TRUE

Front 147

a downhill reaction is __

Back 147

exothermic

Front 148

an uphill reaction is __

Back 148

endothermic

Front 149

free energy doesn't change with catalyst…catalysts only reduce activation energy

Back 149

TRUE

Front 150

part if the 3d protein strucutre where the substrate comes to bind

Back 150

activation site

Front 151

temperature, amount of substrate, and ph level affects __ speed

Back 151

enzyme speed

Front 152

__ results in a conformational change in the enzyme

Back 152

substrate binding; substrate binding results in a conformational change in the enzyme

Front 153

Factors affecting the reaction velocity include:

Back 153

substrate concentration, temperature, and ph

Front 154

the higher the substrate concentration the ___ the reaction

Back 154

faster; the higher the substrate concentration, the faster the reaction

Front 155

__ is the number of molecules of substrate converted to product per minute

Back 155

V; velocity of reaction is the number of molecules of substrate converted to product per minute

Front 156

velocity increases as substrate increases until ___ is reached

Back 156

Vmax; velocity increases as substrate increases until maximum velocity is reached

Front 157

__ reflects the saturation of enzymes binding sites with substrates

Back 157

vmax; maximum velocity reflects the saturation of enzyme binding sites with substrates

Front 158

velocity __ with temperature until vmax is reached

Back 158

increases; velocity increases with temperature until vmax is reached

Front 159

if temp increases too much, velocity will decrease due to ___

Back 159

protein denaturation; if temperature increases too much, velocity will decrease due to protein denaturation

Front 160

ph affects ionization of ___

Back 160

active site; ph affects ionization of active site

Front 161

optimum ph varies for different enzymes; for instance, alkaline phosphatase which is found in blood and tissues likes a ___ ph

Back 161

high ph; alkaline phosphidase which is found in blood and tissue likes a high ph

Front 162

pepsin, found in the stomach likes a __ ph

Back 162

low ph; pepsin found in the stomach likes a low ph b/w 2-3

Front 163

trypsin likes a __ ph

Back 163

neutral; trypsin likes a neutral ph of 6.5

Front 164

describes how reaction velocity varies with substrate concentration

Back 164

michaelis-menten equation describes how reaction velocity varies with substrate concentration

Front 165

the michaelis constant is

Back 165

Km

Front 166

Km reflect the __ of an enzyme for a substrate

Back 166

affinity; km reflects the affinity of an enzyme for a substrate

Front 167

km=

Back 167

km=1/2 Vmax

Front 168

every enzyme has a unique km

Back 168

TRUE

Front 169

__ predicts the velocity of a reaction

Back 169

km; km predicts the velocity of a reaction

Front 170

in the micahelis menton equation, the enzyme concentration remains constant, but the __ concentration is modified

Back 170

substrate concentration; michaelis mention equation keeps enzyme concentration constant and modifies the substrate concentration

Front 171

michaelis menten has a __ curve

Back 171

hyperbolic, a hyperbolic curve represents michaelis-mention equation

Front 172

a small km means the enzyme has a __ affinity for the substrate

Back 172

high; a small km means the enzyme has a high affinity for the substrate b/c it only takes a little bit of substrate for reaction to reach 1/2vmax

Front 173

large km means __ affinity b/w substrate and enzyme

Back 173

low ; a large km reflects a low affinity b/w substrate and enzyme b/c it means it takes a lot of substrate to reach 1/2 vmax

Front 174

__ occurs when inhibitor binds reversibly to active site of enzyme, therby competing with S for binding at that site

Back 174

competitive inhibition; competitive inhibition occurs when an inhibitor binds reversibly to an enzymes active site and thusly competes with the substrate for that binding site

Front 175

in competetive inhibition, __ is not affected

Back 175

in competetive inhibition, vmax is not affected because can overcome inhibition by adding more substrate

Front 176

in competetiive inhibition, __ increases

Back 176

km; in competitive inhibition km increases

Front 177

competitive inhibition increases km, does not change vmax, and shifts the curve to the __

Back 177

right; competitive inhibition increases km, does not change vmax, and shifts the curve to the right

Front 178

___ occurs when inhibitor and substrate bind at different sites on the enzyme

Back 178

noncompetitive inhibition; noncompetitive inhibition is when inhibitor and substrate bind at different sites on the enzyme

Front 179

vmax is __ by noncompetitive inhibition

Back 179

decreased; vmax is decreased by noncompetitive inhibition

Front 180

__ is not affected with noncompetitive inhibition

Back 180

km; km is not affected by noncompetitive inhibition

Front 181

___ inhibition slow the rate of reaction

Back 181

noncompetitive inhibition; noncompetitive inhibition slows the rate of reaction

Front 182

__ inhibition decreases vmax and 1/2 vmax, and does not affect km

Back 182

noncompetitive inhibition

Front 183

__ inhibition does not affect vmax, and increases km

Back 183

competitive inhibition

Front 184

___ inhibition does not affect vmax and increases km, __ inhibition decreases vmax and 1/2 vmax, and does not affect km;

Back 184

competitive inhibition/noncompetitive inhibition; competitive inhibition does not affect vmax but increases km; noncompetitive inhibition does not affect km but decreases vmax.

Front 185

cyanide, carbonmonoxide, and heavy metals are examples of ___ binding

Back 185

irreversible; carbon monoxide, cyanide, and heavy metals are examples of irreversible binding

Front 186

noncompetitive and competitie inhibitors are examples of ___ binding

Back 186

reversible; competitive and noncompetitive inhibition are examples of reversible binding

Front 187

malonate and ethanol are examples of ___ inhibition

Back 187

competitive inhibition; ethanol and melonate are examples on competitive inhibition

Front 188

isoleucine, which is a feedback inhibitor is an example of __ inhibition

Back 188

noncompetitive; isoleucine is an example of a noncompetitive inhibitor

Front 189

__ is essential for coordination of metabolic processes

Back 189

enzyme regulation

Front 190

___ enzymes don't follow the michaelis-menton curve and instead have a sigmoid curve

Back 190

allosteric enzymes; allosteric enzymes follow a sigmoid curve

Front 191

regulated by either positive or negative effectors that bind to a site other than an active site; alter affinity of E or S or modifying maximum activity of enzyme

Back 191

allosteric enzymes

Front 192

__ effectors inhibit enzyme activity

Back 192

negative effectors; negative effectors inhibit enzyme actiivity

Front 193

__ effectors increase enzyme activity

Back 193

positive effectors; positive effectors inhibit enzyme activity

Front 194

there are homotropic and heterotropic effectors that regulate __ enzymes

Back 194

allosteric; regulators of allosteric enzymes are either homotropic or heterotropic

Front 195

if an allosteric enzyme has a ___ regulator, then S serves as the effector and is typically a positive effector

Back 195

homotropic; S serves as the effector and is typically positive

Front 196

if an allosteric enzyme has a __ regulator, then the effector may be different than S and is usually negative

Back 196

heterotropic; the effector may be different than S and is usually negative

Front 197

binding of asubstrate increases the affinity of other substrates; after 1st binds, the 2nd, 3rd, and 4th binds faster and faster; hemoglobin is an example

Back 197

enzyme cooperativity

Front 198

when the end product of enzyme catalyzed reactions will inhibit the activity of an earlier enzyme in the path

Back 198

feedback inhibition; feedback inhibition is when the endproduct inhibits the activity of an earlier enzyme in the path

Front 199

one way to increase the production of a metabolic end product is by increasing the amount of enzyme present

Back 199

TRUE

Front 200

__ is the synthesis of new enzymes in response to a temporary need of the cell

Back 200

enzyme induction; enzyme induction is the synthesis of new enzymes inr esponse to a temporary need of the cell

Front 201

___ allows the cell to adapt to environmental changes

Back 201

enzyme induction; enzyme induction allows the cell to adapt to environmental changes

Front 202

__ occurs by the addition or removal of phosphate groups

Back 202

covalent modification; covalent modification occurs by the addition or removal of phosphate groups

Front 203

__ is catalyzed by kinases and utilizes ATP as the phospate donor

Back 203

phosphorylation; phosphorylation is catalyzed by kinases and uses ATP

Front 204

__ is catalyzed by phophatases which cleaves phosphate groups from enzymes

Back 204

dephosphorylation; dephosphorylation is catalyzed by phosphatases and cleaves phosphate groups from enzyms

Front 205

The central theme of molecular biology is to describe thr flow of info from DNA through RNA to proteins

Back 205

TRUE

Front 206

genetic info is encoded in ___

Back 206

dna

Front 207

prior to cell division, new DNA is synthesized by complimetary pairing of ___ on 2 dna strands

Back 207

nucleotide bases; prior to cell division new DNA is synthesized by complimentary pairing of nucleotide bases on 2 dna strands

Front 208

__ is involved in decodig dna and translating this info to produce proteins

Back 208

RNA; RNA is involved in decoding dna and translating the info to produce proteins

Front 209

the 3 types of rna are

Back 209

mRNA, tRNA, and rRNA

Front 210

nucleic acids are polymers classified into two categories: ___ and __

Back 210

Ribonucleic acid (RNA ) and Deoxyribonucleic acid (DNA)

Front 211

__ is found mainly in cell cytoplasm

Back 211

RNA; RNA is mainly found in cell cytoplasm

Front 212

__ is mainly found in cell nuclei

Back 212

DNA; dna is found mainly in cell nuclei

Front 213

__ make up nucleic acids

Back 213

nucleotides; nucleotides make up nucleic acids

Front 214

nucleotides are composed of 3 components:

Back 214

nitrogen base, sugar, and phospate; nucleotides are made up of nitrogen base, sugar, and phosphate

Front 215

a __ is just a base and sugar

Back 215

nucleoside; a nucleoside is just a nitrogen base and sugar (does not have phospate group)

Front 216

deoxyribonucleic acid does not have__

Back 216

oxygen

Front 217

nucleotides are composed of pyrimidines and purines, phosphate, and __

Back 217

either ribose or 2-deoxyribose; nucleotides are composed of pyrimidines/purines, phosphate, and either ribose or 2-deoxyribose

Front 218

__ is single stranded, contains ribose sugar, and has uracil instead of thymine

Back 218

RNA; RNA is single stranded, has uracil instead of thymine, and contains ribose sugar

Front 219

__ is double stranded, contains deoxyribose sugar, and has thymine

Back 219

dna; dna is double stranded, has thymine, and contains deoxyribose sugar

Front 220

the 3 pyrimidines are

Back 220

cytosine, thymine, and uracil; cytosine, thymine, and uracil are the 3 pyrimidines

Front 221

the 2 purine are

Back 221

guanine and adenine; guanine and adenine are the 2 purines

Front 222

there are __ pyrimidines and __ purines

Back 222

3/2; there are 3 pyrimidines and 2 purines

Front 223

__ structure has 2 rings

Back 223

purine; purine's structure has 2 rings

Front 224

nucleotide formation is a __ reaction b/c 2 h20 are released

Back 224

condensation; nucleotide formation is a condensation reaction b/c 2 water molecules are released

Front 225

in the formation of the nucleotide, the nitrogen base is in the __ prime position

Back 225

1'; in nucleotide formation, the nitrogen base is in the 1 prime location

Front 226

in the formation of the nucleotide, the phospate group is the the __ prime position

Back 226

5'; in nucleotide formation, the phosphate group is in the 5' position

Front 227

dna and rna are ___

Back 227

polynucleotides

Front 228

there is a ___ linkage b/w 2 nucleotides

Back 228

phosphodiester linkage; linkage b/w two nucleotides is a 3' to 5' phosphodiester bond.

Front 229

dna and RNA sequences are always read from __ prime to __ prime

Back 229

5 prime to 3'; sequences are always read from 5'-->3'

Front 230

in dna, A and __ always bond

Back 230

T; in DNA adenine and thymine always bond

Front 231

in rna A and __ bond

Back 231

U; in RNA adenine bonds with uracil

Front 232

C and __ always bond

Back 232

G; cytosine and guanine always bond

Front 233

human cells contain __ pairs of chromosomes

Back 233

23

Front 234

each chromosome contains one __

Back 234

dna strand

Front 235

dna strand coils around the __ proteins to form a nucleosome

Back 235

histone; dna strand coils aroune the histone proteins to form a nucleosome

Front 236

nucleosomes condense to form __

Back 236

chromatin; nucleosomes condense to form chromatin

Front 237

__ can fold back on itself

Back 237

RNA; RNA can fold back on itself

Front 238

___ syntheizes RNA

Back 238

RNA polymerase; rna polymerase synthesizes RNA

Front 239

transcription happends __ the nucleus

Back 239

inside; transcription happends inside the nucleus

Front 240

the __ controls protein synthesis inside the body

Back 240

nucleus

Front 241

the message that comes from the nucleus is the ___

Back 241

amino acid sequence; the message that comes from the nucleus is the amino acid sequence

Front 242

RNA is found mostly in the __

Back 242

cytoplasm

Front 243

__ is the formation of mRNA from DNA and occurs in the nucleus

Back 243

transcription; transcription is the formation of mRNA from DNA and occurs in the nucleus

Front 244

during transcription the info in the DNA is rewritten into __

Back 244

Mrna

Front 245

DNA unravels, and the available strand of DNA to be read is the ___ strand also known as the template or parent strand

Back 245

sense strand; DNA unravels and the available strand of DNA to be read is the sense strand.

Front 246

once produced by transcription, the ___ leaves the nucleus and goes into the cytoplasm

Back 246

mRNA; once produced by transcription, the mRNA leaves the nucleus and goes into the cytoplasm

Front 247

__ carries info to the ribosome where translation occurs

Back 247

Mrna;Mrna carries info to the ribosome where translation occurs

Front 248

translation occurs outside of the nucleus and on ___

Back 248

ribosomes; translation occurs outside of the cell and on ribosomes