Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

Biochem > Bartling SG > Flashcards

Bartling SG Flashcards

1
Q

Glycine

A

Non-polar, aliphatic AA

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

Alanine

A

Non-polar, aliphatic AA

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

Valine

A

Non-polar, aliphatic AA

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

Isoleucine

A

Non-polar, aliphatic AA

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

Phenylalanine

A

Non-polar, aromatic AA

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

Tyrosine

A

Non-polar, aromatic AA

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

Tryptophan

A

Non-polar, aromatic AA

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

threonine

A

UNCHARGED, POLAR AA

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

Serine

A

UNCHARGED, POLAR AA

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

Asparagine

A

UNCHARGED, POLAR AA

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

Glutamine

A

UNCHARGED, POLAR AA

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

Aspartic Acid

A

ACIDIC AA

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

Glutamic Acid

A

ACIDIC AA

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

Histidine

A

BASIC AA

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

Lysine

A

BASIC AA

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

Arginine

A

BASIC AA

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

Cysteine

A

SULFER CONTAINING AA

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

Methionine

A

SULFER CONTAINING AA

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

Proline

A

CYLIC AA

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

does not form conventional peptide bond

A

Proline

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

aliphatic sidechain w/ no functional groups

A

Proline

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

alpha amino group bonded to side chain

A

Proline

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

sidechain covalently bonds to amide N (eliminating H bond possibility)

A

Proline

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

the AA exists as a dipolar molecule having both + & - charges

A

zwitterion

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

in a zwitterion which group is deprotonated, having a - charge

A

alpha carboxyl group

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

in a zwitterion which group is protonated, having a + charge

A

alpha amino group

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

which AA doesn’t has an asymmetry center and therefore isn’t optically active?

A

glycine

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

at least one center of asymmetry makes most AA’s what?

A

optically active

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

AA sequence, linear polymers linked by peptide bonds is what type protein structure

A

Primary

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

Local folded structures, maintained by H bond networks what type of protein structure

A

Secondary

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

H bonds between backbone amide NH and C=O groups stabilize

A

Alpha Helices

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

Alpha helices and Beta sheets

A

Secondary

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

backbone of polypeptide is extended into zigzag, polypeptide chains arranged side by side

A

Beta Sheets

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

3D structure

A

Tertiary Structure

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

disulfide bonds

A

Tertiary Structure

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

salt bridges

A

Tertiary Structure

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

hydrophobic interactions

A

Tertiary Structure

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

structure of more than one subunit together

A

Quaternary Structure

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

pH which a molecule has no net charge, isoelectric point

A

PI

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

widely used to calculate the isoelectric point of proteins

A

Henderson-Hasselbach

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

carboxyl group accepts a proton and becomes uncharged, overall charge on molecule is positive +

A

Ionization state at low pH

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

amino group loses its proton and becomes uncharged, overall charge on molecule is negative-

A

Ionization state at high pH

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

bond formed between alpha-carboxyl of one AA and the alpha-amino group of another

A

Peptide

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

what is removed in the process of linking AA’s together

A

H2O

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

2 AA’s linked

A

Dipeptide

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

3-10 AA’s

A

Oligopeptide

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

11-99 AA’s

A

Polypeptide

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

100 or more AA’s

A

Protein

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

Abnormal metabolic condition leading to excess levels of homocysteine

A

HOMOCYSTEINURIA

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

result of Homocysteinuria

A

downward dislocation of lens, long limbs, mental retardation, seizures

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

converts sulfite to sulfate

A

sulfate oxidase

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

alternative metabolic pathways for sulfite are used leading to formation of s-sulfocysyeine

A

sulfate oxidase deficiency

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

no disulfide bonding in connective tissue

A

sulfate oxidase deficiency

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

lens dislocation, associated w/ mutations in the fibrillin gene

A

Marfan syndrome

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

Green teeth in children is a result of

A

hyperbilirubinemia

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

precipitation of proteins occurs at high salt concentrations

A

Salting out

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

which separation method uses salting in and salting out?

A

Solubility

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

absorption chromatography is what type of separation method

A

polarity

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

to purify and concentrate biomolecules based on chemical or physical differences

A

Chromatography

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

paper chromatography is what type of separation method

A

polarity

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

reverse-phase chromatography is what type of separation method

A

polarity

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

hydrophobic interactions are used for what type of separation method

A

polarity

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

adjust solution just below point of solubility of protein of interest for separation

A

solubility method

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

Larger molecules flow faster through column, first fractions consist of large and begin to collect smaller in later stages

A

Size exclusion chromatography

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

increased polarity increases rate at which molecules move through the column

A

gel filtration chromatography

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

uses beads to separate proteins based on charge

A

Ion exchange chromatography

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

binds protein w + charge, carboxymehtylcellulose

A

Cation Exchanger

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

DEAE cellulose, binds protein w -

A

Anion Exchanger

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

bind antibody/antigen to protein resin

A

AFFINITY CHROMATOGHRAPY

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

specific interaction of substrate with a ligand & purifies neatly pure product in a single step

A

AFFINITY CHROMATOGHRAPY

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

Typical affinity chromatography interaction

A

antibody - antigen pairs

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

migration of ions in an electric field depending on molecule charge (q) and frictional coefficient (f)

A

electrophoresis

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

Separates proteins on basis of their pI

A

iloelectric focusing (IEF)

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

protein that is in a pH region below its pI (+) will migrate towards the cathode until it stops at its pI; vice versa for protein that is in a pH region above pI (-)

A

iloelectric focusing (IEF)

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

number of sterioisomers

A

2^n

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

chiral variations change what properties

A

chemical, physical and, physiological

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

of the 8 D-aldohexoses which 3 are found significantly in body

A

glucose, mannose, galactose

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

single sugars: starch, cellulose, glycogen

A

Homoglycan

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

More than one sugar: gums, mucopolysaccharides

A

Heterogylcan

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

most common storage polysaccharide in plants

A

Starch

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

animal equivalent to starch

A

glycogen

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

stored in muscle and liver cells as high MW granules

A

glycogen

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

hydrolyzed by amylases and glycogen phosphorylase

A

glycogen

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

glucosamine is what?

A

amino sugar

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

why has glucose been selected by evolution for the base sugar of blood?

A

inertness/ not reactiveness

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

relatively un-reactive

A

glucose

87
Q

what is the most abundant carbohydrate in nature

A

Cellulose

88
Q

extractable by non polar solvents

A

lipids

89
Q

fats, waxes, sterols, mono-di-glycerides, phospholipids

A

lipids

90
Q

originate from ketoacyl and isoprene groups

A

lipids

91
Q

simplest form of lipids

A

fatty acids

92
Q

found primarily in plasma

A

fatty acids

93
Q

solid storage form of lipids

A

triglycerides

94
Q

primarily found in adipose tissue

A

triglycerides

95
Q

major class of membrane lipids in a cell

A

phospholipids

96
Q

largely determined by the length and degree of unsaturation of the hydrocarbon chain

A

physical properties of fatty acids

97
Q

Carboxylic acids with a long aliphatic chain

A

fatty acid

98
Q

what decreases with increasing length of a fatty acid chain?

A

solubility in water

99
Q

what makes a kink in the linear structure of fatty acids?

A

cis double bonds

100
Q

the most stable arrangement is very close packing of the side chains

A

saturated lipids

101
Q

the carboxylic end of a fatty acid is ____ making it ____

A

Polar, Moderately water soluble

102
Q

Fatty acids are esterified to glycerol to form?

A

triglycerides

103
Q

What molecule is central to both carbohydrate and fat metabolism?

A

Acetyl-coA

104
Q

Used as STORAGE FUEL

A

Triacylglyerols

105
Q

______ has more energy present, are more “reduced” than cabs and not hydrated by water than ____

A

Fatty acids, polysaccharides

106
Q

polar lipids derived from phosphatidic acid (1,2-diacyl-glycerol-3-phosphate)

A

phospholipids

107
Q

long chain amino alcohol that does not has a glycerol backbone

A

Sphingolipids

108
Q

Found largely in the outer face of plasma membranes

A

Sphingolipids

109
Q

Involved as cell surface recognition sites

A

Sphingolipids

110
Q

how to fatty acids bond to the Sphingolipids, which is unlike the bonding in glycerol?

A

amine linkage

111
Q

sulfuric acid ester of galactocebroside

A

SULFATIDES

112
Q

brain lipids, present in low levels in liver, lung, kidney, spleen, skeletal muscle, and heart

A

SULFATIDES

113
Q

cell to cell regonition, hormone receptors

A

GANGLIOSIDES

114
Q

complex glycosphingolipid

A

GANGLIOSIDES

115
Q

responsible for inflammation in asthma an bronchitis and anaphylaxis

A

LEUKOTRIENES

116
Q

also found in lung, spleen, brain, and heart

A

Leuktoreines

117
Q

particles found in plasma that transport lipids including cholesterol

A

Lipoproteins

118
Q

what does the liver repackages cholesterol into?

A

Lipoproteins

119
Q

what takes lipids from small intestine into lymph cells

A

Chylomicrons

120
Q

what are proteins with covalently attached lipids?

A

lipid-linked proteins

121
Q

what are the three types of lipid-linked proteins

A

Prenylated proteins
Fatty acylated proteins
GPI linked proteins

122
Q

What molecule is central to both carbohydrate and fat metabolism?

A

Acetyl-CoA

123
Q

what is determined in part by the type of sugars located on head groups

A

Blood groups

124
Q

what is esterified to glycerol to form Triglycerides?

A

Fatty Acids

125
Q

what enzyme breaks down dietary fats into smaller molecules called fatty acids and glycerol

A

Lipase

126
Q

do lipids or carbohydrates yield more energy?

A

Lipids

127
Q

diffusion that uses no energy and molecules move from high concentration to low

A

Simple diffusion

128
Q

small hydrophobic molecules cross the cell membrane by

A

simple diffusion

i.e. lipids O2 CO2

129
Q

Movement of specific molecules down a concentration gradient, passing through the membrane via a specific carrier protein

A

Facilitated Diffusion

130
Q

if the carrier protein of facilitated diffusion ever open all the way through?

A

No

131
Q

is energy used in facilitated diffusion?

A

No

132
Q

what types of molecules diffuse using a carrier protein

A

polar, hydrophilic molecules

133
Q

the greater the difference in concentration on either side of a membrane does what to the rate of diffusion?

A

increases

134
Q

diffusion is faster at higher or lower temperatures?

A

higher, more genetic energy

135
Q

does increases surface area increase rate of diffusion?

A

yes

136
Q

non polar or polar molecules diffuse faster?

A

non-polar

137
Q

large molecules diffuse ..

A

slowly

138
Q

uses ATP to drive molecules across the cell membrane

A

Active transport

139
Q

Moves molecules against concentration gradient

A

Active transport

140
Q

uses ATP dependent ion pumps

A

Primary active transport

141
Q

passive transport of water moving freely in and out of the cell

A

osmosis

142
Q

use electrochemical gradient of Na+ or H+ ions, or a membrane potential produced by primary active transport processes (sugars, aa)

A

secondary active transport

143
Q

types of secondary transport

A

Uniport
Symport
Antiport

144
Q

transport of a single solute

A

Uniport

145
Q

2 different ions/molecules being transported at the same time but in opposite directions

A

antiport

146
Q

caries two dissimilar solutes/substrates and transports them together

A

symport

147
Q

GLUT1 glucose carrier in plasma membranes

A

Secondary active (uniport)

148
Q

Glucose-NA

A

secondary active (symport)

149
Q

Lactose permease

A

secondary active (H+ symport)

150
Q

The energy value of fuels (calorie content) is calculated for the complete oxidation of the fuel

A

fuel/ calorie relationship

151
Q

more reduced fuels (need more oxidizing) have …

A

higher calorie/g

152
Q

Fats cals/g

A

9

153
Q

alcohol cals/g

A

7

154
Q

carbs cals/g

A

4

155
Q

proteins cals/g

A

4

156
Q

an estimate of how many calories you’d burn if you were to do nothing but rest for 24 hours

A

Basal Metabolic Rate (BMR)

157
Q

represents the minimum amount of energy needed to keep your body functioning, including breathing and keeping your heart beating

A

Basal Metabolic Rate (BMR)

158
Q

what percent of energy from food is converted into ATP?

A

40%

159
Q

what percent of energy from food is lost as heat?

A

60%

160
Q

what accounts for most of BMR

A

heat production by mitochondria

161
Q

the maximal amount of energy that can be obtained from a reaction at constant temperature and pressure

A

Gibb’s free energy

162
Q

free energy content of the final state minus the free energy content of the initial state

A

Gibb’s free energy

163
Q

spontaneous, favorable rxn

A

Neg. Delta G

164
Q

non-spontatious, unfavorable rxn

A

Pos. Delta G

165
Q

how does ATP drive “uphill” rxns

A

when hydrolyzed ATP yield large neg delta G, allows unfavorable rxn to occur

166
Q

for the reverse of Hydrolyzing glucose-6-phosphate into glucose and pyruvate to occur what must it be coupled with?

A

hydrolysis of ATP to ADP

167
Q

how is the outer membrane of mitochondria different from the inner

A

outer: very permeable to ions & proteins
inner: impermeable to most things w/o carrier protein

168
Q

what membrane of mitochondria contains components of oxidative phosphorylation (process of coupling oxidation of reduced nucleotide coenzymes to synthesis of ATP)

A

inner membrane

169
Q

3 main Coenzymes

A

NAD+
FAD
FMD

170
Q

Coenzymes NAD+ is used in what complex?

A

Complex I

171
Q

Coenzymes FAD is used in what complex

A

complexes II, III, IV

172
Q

coenzymes FMD is used in what complex

A

complex I

173
Q

found in mito and ER, proteins that contain large heme groups but are not involved in oxygen transport

A

Cytochromes

174
Q

inhibits respiration via proton channel of ATP synthase

A

Oligomycin

175
Q

Shuttles e-‘s from complex III to complex IV

A

cytochrome C

176
Q

how many cytochrome C molecules are required from reducing O2 to H2O in complex VI

A

4 b/c it only carries 1 e-

177
Q

found in mito and ER, proteins that contain large heme groups but are not involved in oxygen transport

A

cytochromes

178
Q

inhibit the coupling between the electron transport and phosphorylation reactions and thus inhibit ATP synthesis without affecting the respiratory chain and ATP synthase

A

uncoupler

179
Q

bind to Hgb and inhibit oxygen transport, electron transport, and production of ATP

A

Mitochondrial Poisons

180
Q

cells respond to this by switching to anaerobic metabolism, resulting in lactic acidosis and eventually death

A

Mitochondrial Poisons

181
Q

what type of poising in CN or CO

A

Mitochondrial Poisons

182
Q

what is a triglyceride

A

storage and transport form of lipids

183
Q

where is triglyceride found?

A

adipose tissue

184
Q

what is triglyceride made of

A

glycerol back bone & fatty acids

185
Q

where isn’t triglyceride stored?

A

RBC’s & Brain

186
Q

where is triglyceride stored?

A

liver, muscles, and tissues

187
Q

how are lipids metabolized in the liver?

A

Acetyl-CoA → Ketone bodies (ketogenesis)

188
Q

how are lipids metabolized in muscles?

A

TCA cycle oxidative phosphorylation for ATP production

189
Q

triglycerides are broken down with

A

lipase

190
Q

how are fats transported

A

chylomicrons

191
Q

what regulated the speed at which triglycerides are hydrolyzed in adipose tissue?

A

hormones

192
Q

where does beta oxidation occur?

A

mitochondria

193
Q

what is a long chain fatty acid?

A

between 12-20 carbons?

194
Q

where are long chain fatty acids metabolized?

A

mitochondria

195
Q

how are long chain fatty acids metabolized?

A

carnitine cycle

196
Q

How is glucose metabolism linked to lipid synthesis

A

Pentose phosphate pathway

197
Q

what does Pentose phosphate pathway provide?

A

NADPH

198
Q

process by which acetyl-coa is converted to fatty acids?

A

Lipogenesis

199
Q

how many steps is Lipogenesis

A

2

200
Q

the formation of malonyl-CoA from acetyl-CoA by acetyl-CoA carboxylase is what step of Lipogenesis

A

stage 1

201
Q

the elongation of the fatty acid chain in two-carbon increments by fatty acid synthase is what step of Lipogenesis

A

stage 2

202
Q

Triacylglycerol synthesis in liver

A

Glycerol kinase + phosphate

203
Q

Triacylglycerol synthesis in fat cells

A

Dihydroxyacetone phosphate

204
Q

what makes G3P

A

Dihydroxyacetone phosphate and Glycerol kinase + phosphate

205
Q

Lipoprotein lipase is produced by?

A

Adipocytes

206
Q

what does Lipoprotein lipase promote?

A

glycolysis (glucose uptake)

207
Q

what does Lipoprotein lipase increase the synthesis of?

A

Triacylglycerol

208
Q

what directs fat metabolism towards synthesis and storage ?

A

insulin

209
Q

what does eating stimulate the production of?

A

insulin

210
Q

Protein solubility increases due to shielding of protein charges

A

salting in, solubility purification

211
Q

Protein solubility decreases with increasing ionic strength, competition for molecules

A

salting out, solubility purification

212
Q

affinity chromatography that is ligand specific and is a single step process

A

Biorecognition

213
Q

What are some ways to characterize proteins by separation methods

A

Size, charge, pH, pI

214
Q

intermediate in the citric acid cycle used by cells to produce energy in the form of adenosine triphosphate (ATP) from food.

A

Fumerate

Biochem (2 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2024 Bold Learning Solutions. Terms and Conditions