Biochem Test 1 Flashcards

1
Q
A
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

nucleoside

A

contains a ribose or deoxyribose + a nitrogen containing base

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

beta

A

if the base is upward

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

nucleotide

A

nucleoside + a phosphate group

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

purine bases

A

adenine, guanine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

purine nucleosides

A

adenosine, guanosine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

pyrimidines

A

cytosine, uracil, thymine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

pyrimidine nucleosides

A

cytidine, uridine, thymidine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

in DNA adenine pairs with

A

thymine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

in DNA guanine pairs with

A

cytosine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

in RNA thymine pairs with

A

uracil

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

polynucleotides make up

A

nucleic acids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

polynucleotides are linked through 3’-5’

A

phosphodiester bonds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

the backbone of nucleic acids are

A

pentose phosphate backbone

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

bases are linked through

A

hydrogen bonding

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

A & T are WEAKER because they only have __ hydrogen bonds where as G & C have _____ hydrogen bonds

A

2, 3

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

____ or ________ can be used as antiviral and cancer drugs

A

nucleoside, base analogues

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

how do analogues work as drugs for cancer or virus

A

they block DNA replication and the virus will be unable to multiply

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

ATP contains 2 ________ that can be hydrolyzed to produce energy for coupled biochemical or cellular processes

A

high-energy phosphate bonds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

one step energy release for ATP =

A

ADP + Pi

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

two step energy release for ATP =

A

AMP + Pi & PPi = 2Pi

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

UTP

A

combining sugars - constantly used

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

CTP

A

lipid synthesis

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

GTP

A

protein synthesis

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
Q

___ ____ & _____ are all energetically equivalent to ATP but specific for different metabolic pathways

A

UTP GTP CTP

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
26
Q

ATP + UDP =

A

ADP + UTP

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
27
Q

ADP + ADP =

A

ATP + AMP

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
28
Q

cellular ATP is main generated through ____ & _____

A

substrate level phosphorylation, oxidative phosphorylation

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
29
Q

ATP that is generated via ATP generating reactions

A

substrate level phosphorylation

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
30
Q

ATP that is generated via electron transport chain

A

oxidative phosphorylation

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
31
Q

GTP cycle is associated with changes in ____ & ____

A

protein conformation & activity

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
32
Q

cAMP

A

important second messenger in cell signaling

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
33
Q

_____ inhibitors blocks the degradation of cAMP

A

phosphodiesterase

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
34
Q

NAD

A

Nicotinamide adenine dinucleotide

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
35
Q

NADP

A

Nicotinamide adenine dinucleotide phosphate

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
36
Q

carbohydrates

A

polyhydroxy aldehydes and ketones

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
37
Q

functions of carbohydrates

A

fuels, regulation, structural components

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
38
Q

caloric contents

A

the ability of a specific carbohydrate to produce energy

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
39
Q

carbohydrates caloric content

A

4 kcal/g

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
40
Q

fat caloric content

A

9 kcal/g

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
41
Q

protein caloric content

A

4 kcal/g

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
42
Q

carbohydrates

A

made of glycogen, present in muscle and liver, store energy for emergency use

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
43
Q

glyceraldehyde

A

a triose - a sugar that contains only three carbon atoms

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
44
Q

a glyceraldehyde is

A

the simplest carbon with only one chiral carbon

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
45
Q

D orientation

A

hydroxyl is on the right

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
46
Q

L orientation

A

hydroxyl is on the left

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
47
Q

enantiomers

A

are mirror image compounds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
48
Q

glucose and most other sugars in human tissues have the ___ configuration

A

D

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
49
Q

stereoisomers

A

the same chemical formula but different 3-D orientation

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
50
Q

Epimers

A

stereoisomers that different in the configuration of only chiral center

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
51
Q

pyranose

A

6 membered ring with oxygen, D orientation, glucose mostly exists in this form

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
52
Q

furanose

A

5 membered ring with oxygen, D orientation

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
53
Q

anomers

A

two forms of the same structure (i.e. cyclic)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
54
Q

CH2OH same side is

A

Beta

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
55
Q

CH2OH opposite side

A

alpha

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
56
Q

mutarotation

A

conversion between anomers

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
57
Q

Oxidized Sugars

A

add drug to make it easier to be metabolized & kidney function

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
58
Q

glucuronidation

A

addition of glucuronate to a substrate

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
59
Q

di & polysaccharides consists of monsaccharides linked through ______

A

O-glycosidic bonds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
60
Q

amylose

A

alpha 1,4

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
61
Q

amylopectin

A

alpha 1,4 & alpha 1,6

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
62
Q

cellulose

A

linear Beta 1,4

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
63
Q

glycogen

A

structure resembles amylopectin - both alpha 1,4 and alpha 1,6

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
64
Q

maltose

A

glucose + glucose alpha 1,4

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
65
Q

Sucrose

A

fructose + glucose

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
66
Q

alpha-amylase

A

endoglucosidase that specifically cleaves the alpha 1,4 glycosidic bond

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
67
Q

Na dependent glucose transporters

A

secondary active transporter

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
68
Q

facilitating glucose transporters

A

the GLUT transport protein

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
69
Q

GLUT 1

A

RBC & Barriers - high affinity

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
70
Q

GLUT 2

A

organs take leftovers - low affinity

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
71
Q

GLUT 4

A

sucks up glucose from blood and relies on insulin; reduces blood glucose levels

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
72
Q

GLUT 4

A

increases absorption of glucose into the muscle

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
73
Q

carbohydrates

A

polyhydroxy aldehydes and ketones

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
74
Q

functions of carbohydrates

A

fuels, regulation, structural components

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
75
Q

caloric contents

A

the ability of a specific carbohydrate to produce energy

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
76
Q

carbohydrates caloric content

A

4 kcal/g

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
77
Q

fat caloric content

A

9 kcal/g

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
78
Q

protein caloric content

A

4 kcal/g

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
79
Q

carbohydrates

A

made of glycogen, present in muscle and liver, store energy for emergency use

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
80
Q

glyceraldehyde

A

a triose - a sugar that contains only three carbon atoms

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
81
Q

a glyceraldehyde is

A

the simplest carbon with only one chiral carbon

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
82
Q

D orientation

A

hydroxyl is on the right

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
83
Q

L orientation

A

hydroxyl is on the left

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
84
Q

enantiomers

A

are mirror image compounds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
85
Q

glucose and most other sugars in human tissues have the ___ configuration

A

D

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
86
Q

stereoisomers

A

the same chemical formula but different 3-D orientation

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
87
Q

Epimers

A

stereoisomers that different in the configuration of only chiral center

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
88
Q

pyranose

A

6 membered ring with oxygen, D orientation, glucose mostly exists in this form

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
89
Q

GLUT 4

A

increases absorption of glucose into the muscle

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
90
Q

GLUT 4

A

sucks up glucose from blood and relies on insulin; reduces blood glucose levels

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
91
Q

GLUT 2

A

organs take leftovers - low affinity

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
92
Q

GLUT 1

A

RBC & Barriers - high affinity

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
93
Q

facilitating glucose transporters

A

the GLUT transport protein

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
94
Q

Na dependent glucose transporters

A

secondary active transporter

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
95
Q

alpha-amylase

A

endoglucosidase that specifically cleaves the alpha 1,4 glycosidic bond

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
96
Q

Sucrose

A

fructose + glucose

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
97
Q

maltose

A

glucose + glucose alpha 1,4

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
98
Q

furanose

A

5 membered ring with oxygen, D orientation

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
99
Q

glycogen

A

structure resembles amylopectin - both alpha 1,4 and alpha 1,6

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
100
Q

cellulose

A

linear Beta 1,4

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
101
Q

amylopectin

A

alpha 1,4 & alpha 1,6

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
102
Q

amylose

A

alpha 1,4

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
103
Q

di & polysaccharides consists of monsaccharides linked through ______

A

O-glycosidic bonds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
104
Q

glucuronidation

A

addition of glucuronate to a substrate

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
105
Q

Oxidized Sugars

A

add drug to make it easier to be metabolized & kidney function

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
106
Q

mutarotation

A

conversion between anomers

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
107
Q

CH2OH opposite side

A

alpha

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
108
Q

CH2OH same side is

A

Beta

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
109
Q

anomers

A

two forms of the same structure (i.e. cyclic)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
110
Q

all naturally occurring fatty acids are in ___ formation

A

cis

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
111
Q

w counts

A

backwards

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
112
Q

:

A

carbons:number of double bond

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
113
Q

transfat

A

not naturally, bad for cholesterol, trans confirmation

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
114
Q

Melting point increases

A

with chain length

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
115
Q

Melting point decreases

A

when number of bonds increase

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
116
Q

saturated

A

no double bonds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
117
Q

unsaturated

A

contains double bonds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
118
Q

triacylglyerols

A

stereospecific; chiral

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
119
Q

unsaturated fats preferable form ester bonds with the ___ carbon of glycerol

A

C2

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
120
Q

the N+ makes the molecule

A

hydrophilic

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
121
Q

the head of the phospholipid is

A

hydrophillic

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
122
Q

the tail of the phospholipid

A

hydrophobic

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
123
Q

all head groups attach to the ____ on phospholipids

A

the phosphate group

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
124
Q

the phosphate group is

A

hydrophilic

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
125
Q

the phosphate group is attached to the in phosphocylglycerols

A

C3

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
126
Q

phospholipids

A

lipid on a membrane, contains a phosphate

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
127
Q

phosphoacylglycerols

A

have the phosphate on C3

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
128
Q

phospholipase A1

A

cuts after the oxygen on C1

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
129
Q

phospholipase A2

A

cuts after the oxygen on C2

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
130
Q

phospholipase C

A

cuts between the oxygen and phosphate leaving the head group and phosphate

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
131
Q

phospholipase D

A

cuts the head group off along with the oxygen

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
132
Q

shingolipids

A

sugars or a head group is added to the hydroxyl group of ceramics to form various sphingolipids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
133
Q

phosphoshingolipids

A

attached to a phosphate

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
134
Q

steroids

A

very hydrophobic with a 1 hydrophilic -OH group

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
135
Q

amino acids contain

A

an amino group, alpha carbon, carboxylic acid and side chain

136
Q

amino acids are building blocks for ___ and _____

A

peptides & proteins

137
Q

all amino acids in mammals have the ___ configuration

A

L

138
Q

higher ka = _____ pka = ______

A

lower , more easily deprotonated

139
Q

Ka

A

dissociation constant

140
Q

pH

A

-log[H+]

141
Q

pKa

A

-logKa

142
Q

ka

A

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

143
Q

pka (practical definition)

A

the pH at which half of an acid or conjugate acid is deprotonated

144
Q

at physiological pH free amino acids exist largely as _____

A

zwitterions

145
Q

the structural and fuctional diversity of proteins is ultimately defined by the structural diversity of amino acid _____

A

side chain

146
Q

non polar aliphatic amino acids

A

have non-aromatic hydrocarbon side chains

147
Q

which has a kink in the backbone

A

proline

148
Q

what is the pka for a carboxyl

A

2

149
Q

what is the pka for an amino

A

10

150
Q

higher hydropathy index means

A

more hydrophobic (typically more bulky)

151
Q

hydrophobic side chains are responsible for the ______ which is defined as the observed tendency of hydrophobic groups to cluster together in aqueous environment

A

hydrophobic effect

152
Q

arginine side chain has a

A

guanidinium group

153
Q

histidine side chain contain an

A

imidazole ring

154
Q

which is the major charge contributor of a long peptide or protein

A

side chain

155
Q

the charge of amino acid depends on ____

A

its environment

156
Q

isoelectric point

A

is defined as the pH at which the net charge of a molecule in a solution equals to zero; is a characteristic of a specific amino acid or a protein and does not depend on the chemical environment around the molecule

157
Q

disulfide bonds are responsible for

A

maintaining structural integrity of proteins and peptides

158
Q

cystinuria

A

caused by a genetic defect in a transporter involved in amino acid reabsorption; has low solubility and precipitate in the urine to form kidney stones

159
Q

essential amino acids

A

nine amino acids are essential in the diet of human adults

160
Q

essential amino acids

A

nine amino acids are essential in the diet of human adults

161
Q

cystinuria

A

caused by a genetic defect in a transporter involved in amino acid reabsorption; has low solubility and precipitate in the urine to form kidney stones

162
Q

disulfide bonds are responsible for

A

maintaining structural integrity of proteins and peptides

163
Q

isoelectric point

A

is defined as the pH at which the net charge of a molecule in a solution equals to zero; is a characteristic of a specific amino acid or a protein and does not depend on the chemical environment around the molecule

164
Q

the charge of amino acid depends on ____

A

its environment

165
Q

which is the major charge contributor of a long peptide or protein

A

side chain

166
Q

histidine side chain contain an

A

imidazole ring

167
Q

arginine side chain has a

A

guanidinium group

168
Q

hydrophobic side chains are responsible for the ______ which is defined as the observed tendency of hydrophobic groups to cluster together in aqueous environment

A

hydrophobic effect

169
Q

higher hydropathy index means

A

more hydrophobic (typically more bulky)

170
Q

what is the pka for an amino

A

10

171
Q

what is the pka for a carboxyl

A

2

172
Q

which has a kink in the backbone

A

proline

173
Q

non polar aliphatic amino acids

A

have non-aromatic hydrocarbon side chains

174
Q

the structural and fuctional diversity of proteins is ultimately defined by the structural diversity of amino acid _____

A

side chain

175
Q

at physiological pH free amino acids exist largely as _____

A

zwitterions

176
Q

pka (practical definition)

A

the pH at which half of an acid or conjugate acid is deprotonated

177
Q

ka

A

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

178
Q

pKa

A

-logKa

179
Q

pH

A

-log[H+]

180
Q

Ka

A

dissociation constant

181
Q

higher ka = _____ pka = ______

A

lower , more easily deprotonated

182
Q

all amino acids in mammals have the ___ configuration

A

L

183
Q

amino acids are building blocks for ___ and _____

A

peptides & proteins

184
Q

amino acids contain

A

an amino group, alpha carbon, carboxylic acid and side chain

185
Q

messenger RNA

A

template for protein synthesis

186
Q

transfer RNA

A

carries amino acids to growing peptide

187
Q

ribosomal RNA

A

RNA component of ribosome (protein synthesis)

188
Q

heat duration

A

breaks hydrogen bonds

189
Q

melting temperature

A

at which half of DNA is denatured

190
Q

annealing or renaturation

A

gradually cooling

191
Q

enzyme known as _____ ca relieve the stress caused by supercoiling to allow DNA unwinding

A

toposiomersases

192
Q

nucleosomes

A

nucleosome core + DNA + histone H1

193
Q

solenoid structure

A

nucleosomes wind into helical tubular coils

194
Q

nonhistone chromosomal proteins

A

enzymes acting on DNA and transcriptional factors also associate with DNA

195
Q

why do we package our DNA

A

protection regulations

196
Q

genetic

A

the fundamental unit of heredity

197
Q

structural definition

A

encompasses the DNA sequence that encodes the structural components of the gene product together with its 5’ end adjacent regulatory region

198
Q

genetic locus

A

a specific location on a chromosome

199
Q

allele

A

alternative versions of the same gene in a diploid

200
Q

homozygous

A

having two identical alleles in a dipoloid

201
Q

heterozygous

A

having two different alleles in adiploid

202
Q

dominant trait

A

an inherited characteristic that appears in a diploid offspring if only one copy of the corresponding allele is present. the trait of the other allele is know as recessive

203
Q

intron

A

non-coding genomic sequence within a gene

204
Q

exon

A

coding genomic sequence within a gene

205
Q

double helix

A

single stranded; intra-chain base pairing to form loop structures for binding to proteins or other regions of RNA

206
Q

mRNA

A

provides template

207
Q

codon

A

a sequence of three nucleotide that together form a unit of genetic code in a DNA or RNA molecule

208
Q

prokaryotic ribosomes

A

70s

209
Q

eukaryotic cytoplasmic ribosomes

A

80s

210
Q

mitochondrial ribosomes

A

55s

211
Q

peptide transferase

A

form peptide bond inside ribosome

212
Q

oligoribonucleotides

A

serve as primers during DNA replication

213
Q

small nuclear ribonucleoprotiens

A

are involved in mRNA maturation

214
Q

microRNAs

A

participate in regulation of gene expression

215
Q

heterozygous

A

having two different alleles in adiploid

216
Q

dominant trait

A

an inherited characteristic that appears in a diploid offspring if only one copy of the corresponding allele is present. the trait of the other allele is know as recessive

217
Q

intron

A

non-coding genomic sequence within a gene

218
Q

exon

A

coding genomic sequence within a gene

219
Q

double helix

A

single stranded; intra-chain base pairing to form loop structures for binding to proteins or other regions of RNA

220
Q

mRNA

A

provides template

221
Q

codon

A

a sequence of three nucleotide that together form a unit of genetic code in a DNA or RNA molecule

222
Q

prokaryotic ribosomes

A

70s

223
Q

eukaryotic cytoplasmic ribosomes

A

80s

224
Q

mitochondrial ribosomes

A

55s

225
Q

peptide transferase

A

form peptide bond inside ribosome

226
Q

oligoribonucleotides

A

serve as primers during DNA replication

227
Q

small nuclear ribonucleoprotiens

A

are involved in mRNA maturation

228
Q

microRNAs

A

participate in regulation of gene expression

229
Q

ribosomal RNA

A

RNA component of ribosome (protein synthesis)

230
Q

heat duration

A

breaks hydrogen bonds

231
Q

melting temperature

A

at which half of DNA is denatured

232
Q

annealing or renaturation

A

gradually cooling

233
Q

enzyme known as _____ ca relieve the stress caused by supercoiling to allow DNA unwinding

A

toposiomersases

234
Q

nucleosomes

A

nucleosome core + DNA + histone H1

235
Q

solenoid structure

A

nucleosomes wind into helical tubular coils

236
Q

nonhistone chromosomal proteins

A

enzymes acting on DNA and transcriptional factors also associate with DNA

237
Q

why do we package our DNA

A

protection regulations

238
Q

genetic

A

the fundamental unit of heredity

239
Q

structural definition

A

encompasses the DNA sequence that encodes the structural components of the gene product together with its 5’ end adjacent regulatory region

240
Q

genetic locus

A

a specific location on a chromosome

241
Q

microRNAs

A

participate in regulation of gene expression

242
Q

small nuclear ribonucleoprotiens

A

are involved in mRNA maturation

243
Q

oligoribonucleotides

A

serve as primers during DNA replication

244
Q

peptide transferase

A

form peptide bond inside ribosome

245
Q

mitochondrial ribosomes

A

55s

246
Q

eukaryotic cytoplasmic ribosomes

A

80s

247
Q

prokaryotic ribosomes

A

70s

248
Q

codon

A

a sequence of three nucleotide that together form a unit of genetic code in a DNA or RNA molecule

249
Q

mRNA

A

provides template

250
Q

double helix

A

single stranded; intra-chain base pairing to form loop structures for binding to proteins or other regions of RNA

251
Q

exon

A

coding genomic sequence within a gene

252
Q

intron

A

non-coding genomic sequence within a gene

253
Q

dominant trait

A

an inherited characteristic that appears in a diploid offspring if only one copy of the corresponding allele is present. the trait of the other allele is know as recessive

254
Q

heterozygous

A

having two different alleles in adiploid

255
Q

homozygous

A

having two identical alleles in a dipoloid

256
Q

allele

A

alternative versions of the same gene in a diploid

257
Q

transfer RNA

A

carries amino acids to growing peptide

258
Q

transfer RNA

A

carries amino acids to growing peptide

259
Q

ribosomal RNA

A

RNA component of ribosome (protein synthesis)

260
Q

heat duration

A

breaks hydrogen bonds

261
Q

melting temperature

A

at which half of DNA is denatured

262
Q

annealing or renaturation

A

gradually cooling

263
Q

enzyme known as _____ ca relieve the stress caused by supercoiling to allow DNA unwinding

A

toposiomersases

264
Q

nucleosomes

A

nucleosome core + DNA + histone H1

265
Q

solenoid structure

A

nucleosomes wind into helical tubular coils

266
Q

nonhistone chromosomal proteins

A

enzymes acting on DNA and transcriptional factors also associate with DNA

267
Q

why do we package our DNA

A

protection regulations

268
Q

microRNAs

A

participate in regulation of gene expression

269
Q

small nuclear ribonucleoprotiens

A

are involved in mRNA maturation

270
Q

oligoribonucleotides

A

serve as primers during DNA replication

271
Q

peptide transferase

A

form peptide bond inside ribosome

272
Q

mitochondrial ribosomes

A

55s

273
Q

eukaryotic cytoplasmic ribosomes

A

80s

274
Q

prokaryotic ribosomes

A

70s

275
Q

codon

A

a sequence of three nucleotide that together form a unit of genetic code in a DNA or RNA molecule

276
Q

mRNA

A

provides template

277
Q

double helix

A

single stranded; intra-chain base pairing to form loop structures for binding to proteins or other regions of RNA

278
Q

exon

A

coding genomic sequence within a gene

279
Q

intron

A

non-coding genomic sequence within a gene

280
Q

dominant trait

A

an inherited characteristic that appears in a diploid offspring if only one copy of the corresponding allele is present. the trait of the other allele is know as recessive

281
Q

heterozygous

A

having two different alleles in adiploid

282
Q

homozygous

A

having two identical alleles in a dipoloid

283
Q

allele

A

alternative versions of the same gene in a diploid

284
Q

genetic locus

A

a specific location on a chromosome

285
Q

structural definition

A

encompasses the DNA sequence that encodes the structural components of the gene product together with its 5’ end adjacent regulatory region

286
Q

genetic

A

the fundamental unit of heredity

287
Q

messenger RNA

A

template for protein synthesis

288
Q

messenger RNA

A

template for protein synthesis

289
Q

homozygous

A

having two identical alleles in a dipoloid

290
Q

allele

A

alternative versions of the same gene in a diploid

291
Q

genetic locus

A

a specific location on a chromosome

292
Q

structural definition

A

encompasses the DNA sequence that encodes the structural components of the gene product together with its 5’ end adjacent regulatory region

293
Q

genetic

A

the fundamental unit of heredity

294
Q

why do we package our DNA

A

protection regulations

295
Q

nonhistone chromosomal proteins

A

enzymes acting on DNA and transcriptional factors also associate with DNA

296
Q

solenoid structure

A

nucleosomes wind into helical tubular coils

297
Q

nucleosomes

A

nucleosome core + DNA + histone H1

298
Q

enzyme known as _____ ca relieve the stress caused by supercoiling to allow DNA unwinding

A

toposiomersases

299
Q

annealing or renaturation

A

gradually cooling

300
Q

melting temperature

A

at which half of DNA is denatured

301
Q

heat duration

A

breaks hydrogen bonds

302
Q

ribosomal RNA

A

RNA component of ribosome (protein synthesis)

303
Q

transfer RNA

A

carries amino acids to growing peptide

304
Q

messenger RNA

A

template for protein synthesis

305
Q

peptide bond

A

has double bond character; does not allow for rotation

306
Q

which form cis/trans is more favorable for amino acids

A

trans

307
Q

primary structure

A

the amino acid sequence; overall conformation

308
Q

conservative mutation

A

protein structure is not that different; (ie same charge & similar side chains)

309
Q

non-conservative mutation

A

large difference in side chains (can cause disease)

310
Q

polymorphisms

A

changes in primary structure that may slightly change function (generally tolerable & not disease causing)

311
Q

tissue specific isoforms

A

a protein that has a similar structure and function as another but come from different genes

312
Q

species specific variations

A

insulin (pig cow) or antibodies (mice)

313
Q

developmental variations

A

fetal hemoglobin with higher affinity than adult hemoglobin

314
Q

secondary structures

A

localized regions or segments of the peptide chain that fold into specific patterns that are stabilized by intramolecular forces such as hydrogen bonding

315
Q

alpha helix

A

a rod like structure in which a tightly coiled backbone forms the inner part and the R groups extend outward into a helical array

316
Q

in a helices where does the hydrogen bonding occur

A

4 apart

317
Q

how is a helices oriented

A

clockwise, from n terminus top; spiraling; tightly compacted; rod like with R groups pointed outward

318
Q

which AA are referred to as “helix breakers”

A

proline and glycine

319
Q

Beta pleated sheets

A

more spread out; hydrogen bonding in parallel or antiparallel fashion; made up of 2 or more beta strands

320
Q

non repetitive secondary structures include

A

beta hooks (4) and omega loops (10ish) that connect alpha & beta or 2 of the same

321
Q

motifs

A

small arrangements of secondary structures that are observed in many different proteins; allow for interactions; contain basic amino acids held in place by larger parts of the protein.

322
Q

tertiary structure

A

the overall folding pattern; interior is hydrophobic while exterior is hydrophilic;

323
Q

what types of bonding occurs in tertiary structure

A

hydrogen; salt bridges between charged side chains; van Der walls; ring stacking; disulfide bonds

324
Q

Quaternary structure

A

assembly of multiple individual polypeptide chains into a geometrically and stoichiometric manner

325
Q

2 identical subunits

A

homodimer

326
Q

3 distinct subunits

A

heterotrimer

327
Q

domain

A

can stand alone; superfamily of structures; umbrella containing motifs

328
Q

different types of protein denaturation

A

heat/high temperature; low or high pH; alcohol; hydrophobic molecules/surfactants; chaotropic agents; heavy metals

329
Q

what is the primary determinate of 3D structure

A

sequence of amino acids

330
Q

chaperonins

A

stablize to make it fold correctly; help it get enough energy to go to its native state

331
Q

native confirmation

A

low energy state

332
Q

cis-trans isomerase

A

change the conformation of proline by making it cis so it can have hair pin turns

333
Q

disulfide isomerase

A

breaks bond then the bond reform after proper folding has occurred

334
Q

prion proteins

A

normal proteins found in the human body; a helix is the most dominant form

335
Q

alzheimers

A

small petite fragment; gain of toxicity; neuronal degeneration; huge plaques form

336
Q

cystic fibrosis

A

loss of function; can’t get CFTR into the cell membranes; phenylalanine is deleted